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Prison cell and macromolecules

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Prison cell and macromolecules FOR PHARM.DTHIRD year

Jail cell and macromolecules FOR PHARM.DTHIRD year

  1. 1. The Jail cell The bones unit of life 1sanjukaladharan
  2. 2. Appoint: Cell History • Cytology- report of cells • 1665 English Scientist Robert Hooke • Used a microscope to examine cork (plant) • Hooke called what he saw "Cells" 2sanjukaladharan
  3. 3. Prison cell History • Robert Brown – discovered the nucleus in 1833. • Matthias Schleiden – German Botanist Matthias Schleiden – 1838 – ALL PLANTS "ARE COMPOSED OF CELLS". • Theodor Schwann – Also in 1838, – discovered that animals were made of cells 3sanjukaladharan
  4. iv. Cell History • Rudolf Virchow – 1855, German Physician – " THAT CELLS But COME FROM OTHER CELLS". • His statement debunked "Theory of Spontaneous Generation" 4sanjukaladharan
  5. 5. Jail cell Theory • The COMBINED work of Schleiden, Schwann, and Virchow make up the modern Prison cell THEORY. 5sanjukaladharan
  6. 6. 1. All living things are composed of a jail cell or cells. ii. Cells are the bones unit of measurement of life. three. All cells come from preexisting cells. The Cell Theory states that: 6sanjukaladharan
  7. vii. Prokaryotic Prison cell Cell membrane Prison cell membrane Cytoplasm Cytoplasm Nucleus Organelles Eukaryotic Cell Internal Arrangement 7sanjukaladharan
  8. eight. Prokaryotes Eukaryotes Jail cell membrane Incorporate DNA Ribosomes Cytoplasm Nucleus Endoplasmic reticulum Golgi apparatus Lysosomes Vacuoles Mitochondria Cytoskeleton Compare and Contrast 8sanjukaladharan
  9. 9. Prokaryotic Examples ONLY Bacteria 9sanjukaladharan
  10. 10. EUKARYOTIC CELLS Two Kinds: Institute and Beast 10sanjukaladharan
  11. 11. Eukaryotic Case 11sanjukaladharan
  12. 12. Plant Cell Nuclear envelope Ribosome (attached) Ribosome (free) Smooth endoplasmic reticulum Nucleus Rough endoplasmic reticulum Nucleolus Golgi apparatus Mitochondrion Prison cell wall Jail cell Membrane Chloroplast Vacuole Section vii-ii 12sanjukaladharan
  13. 13. Animate being Cells Institute Cells Centrioles Cell membrane Ribosomes Nucleus Endoplasmic reticulum Golgi apparatus Lysosomes Vacuoles Mitochondria Cytoskeleton Cell Wall Chloroplasts Compare and Contrast Venn Diagrams 13sanjukaladharan
  14. xiv. "Typical" Brute Prison cell http://web.jjay.cuny.edu/~acarpi/NSC/images/cell.gif 14sanjukaladharan
  15. fifteen. Internal Organisation • Cells contain ORGANELLES. • Jail cell Components that PERFORMS SPECIFIC FUNCTIONS FOR THE CELL. 15sanjukaladharan
  16. xvi. Cellular Organelles • The Plasma membrane – The purlieus of the cell. – Composed of iii distinct layers. – Two layers of fat and one layer of poly peptide. 16sanjukaladharan
  17. 17. • it is composed mainly of a lipid bilayer of phospholipid molecules, but with large numbers of poly peptide molecules protruding through the layer. • Two types of proteins occur: integral proteins that protrude all the manner through the membrane, and peripheral proteins that are attached only to one surface of the membrane and do not penetrate all the way through. • Also, saccharide moieties are attached to the protein molecules on the outside of the membrane and to additional poly peptide molecules on the inside. 17sanjukaladharan
  18. 18. The Nucleus • Brain of Cell • Bordered past a porous membrane - nuclear envelope. • Contains thin fibers of Deoxyribonucleic acid and protein called Chromatin. • Rod Shaped Chromosomes • Contains a modest round nucleolus – produces ribosomal RNA which makes ribosomes. 18sanjukaladharan
  19. 19. Nucleoli • The nuclei of most cells contain ane or more highly staining structures chosen nucleoli. • it is only an accumulation of large amounts of RNA and proteins of the types establish in ribosomes. • The nucleolus becomes considerably enlarged when the cell is actively synthesizing proteins. 19sanjukaladharan
  20. twenty. Ribosomes • Small non-membrane leap organelles. • Contain two sub units • Site of protein synthesis. • Poly peptide factory of the jail cell • Either free floating or attached to the Endoplasmic Reticulum. 20sanjukaladharan
  21. 21. 21sanjukaladharan
  22. 22. Endoplasmic Reticulum • Complex network of ship channels. • Ii types: i. Smooth- ribosome complimentary and functions in poison detoxification. 2. Rough - contains ribosomes and releases newly made protein from the prison cell. 22sanjukaladharan
  23. 23. 23sanjukaladharan
  24. 24. Golgi Apparatus • A series of flattened sacs that modifies, packages, stores, and transports materials out of the cell. • Works with the ribosomes and Endoplasmic Reticulum. 24sanjukaladharan
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  26. 26. Lysosomes • Recycling Center – Recycle cellular debris • Membrane bound organelle containing a diversity of enzymes. • Internal pH is five. • Help digest nutrient particles inside or out side the cell. 26sanjukaladharan
  27. 27. Centrioles • Found only in animal cells • Paired organelles found together about the nucleus, at right angles to each other. • Function in building cilia and flagella • Play a role in cellular reproduction 27sanjukaladharan
  28. 28. Jail cell membrane Endoplasmic reticulum Microtubule Microfilament Ribosomes Mitochondrion Cytoskeleton 28sanjukaladharan
  29. 29. Cytoskeleton • Framework of the cell • Contains small microfilaments and larger microtubules. • They back up the cell, giving it its shape and help with the movement of its organelles. • The fibrillar proteins of the cell are usually organized into filaments or tubules. • These originate as precursor protein molecules synthesized past ribosomes in the cytoplasm. • The precursor molecules then polymerize to form filaments. • Eg microtubules 29sanjukaladharan
  30. thirty. Mitochondrion • Double Bleary • It'south the size of a bacterium • Contains its own DNA; mDNA • Produces high energy compound ATP 30sanjukaladharan
  31. 31. 31sanjukaladharan
  32. 32. The Vacuole • Sacs that help in nutrient digestion or helping the cell maintain its water balance. • Establish mostly in plants and protists. • Smaller i in brute prison cell 32sanjukaladharan
  33. 33. sanjukaladharan 33
  34. 34. The FOUR Classes of Big Biomolecules • All living things are made up of four classes of large biological molecules: • Carbohydrates • Lipids • Poly peptide • Nucleic Acids • Macromolecules are large molecules equanimous of thousands of covalently bonded atoms • Molecular construction and function are inseparable 34sanjukaladharan
  35. 35. Macromolecules 35sanjukaladharan
  36. 36. 36sanjukaladharan
  37. 37. Nucleic acid sanjukaladharan 37
  38. 38. The central dogma of molecular biology. 38sanjukaladharan
  39. 39. sanjukaladharan 39 28.11 Nucleic Acids and Heredity • Processes in the transfer of genetic information: • Replication: identical copies of Dna are made • Transcription: genetic messages are read and carried out of the prison cell nucleus to the ribosomes, where protein synthesis occurs. • Translation: genetic messages are decoded to brand proteins.
  40. twoscore. Definitions Nucleic acids are polymers of nucleotides In eukaryotic cells nucleic acids are either: Deoxyribose nucleic acids (DNA) Ribose nucleic acids (RNA) Messenger RNA (mRNA) Transfer RNA (tRNA) Ribosomal RNA (tRNA) Nucleotides are carbon ring structures containing nitrogen linked to a v-carbon sugar (a ribose) 5-carbon sugar is either a ribose or a deoxy-ribose making the nucleotide either a ribonucleotide or a deoxyribonucleotide 40sanjukaladharan
  41. 41. Nucleic Acid Office Deoxyribonucleic acid Genetic cloth - sequence of nucleotides encodes different amino acid RNA Involved in the transcription/translation of genetic material (Dna) Genetic cloth of some viruses 41sanjukaladharan
  42. 42. Nucleotide Structure Despite the complexity and diversity of life the structure of DNA is dependent on only 4 dissimilar nucleotides Diversity is dependent on the nucleotide sequence All nucleotides are 2 ring structures composed of: 5-carbon carbohydrate : β-D-ribose (RNA) β-D-deoxyribose (Deoxyribonucleic acid) Base of operations Purine Pyrimidine Phosphate group A nucleotide WITHOUT a phosphate group is a NUCLEOSIDE 42sanjukaladharan
  43. 43. 43sanjukaladharan
  44. 44. Names of Nucleosides and Nucleotides 44sanjukaladharan
  45. 45. base ( purine 、 pyrimdine ) +ribose ( deoxyribos Due north-glycosyl linkage nucleoside+phosphate phosphoester linkage nucleotide phosphodiester linkage 45sanjukaladharan
  46. 46. Functions of Nucleotides and Nucleic Acids • Nucleotide Functions: – Energy for metabolism (ATP) – Enzyme cofactors (NAD+ ) – Point transduction (army camp) • Nucleic Acid Functions: – Storage of genetic info (Deoxyribonucleic acid) – Manual of genetic info (mRNA) – Processing of genetic data (ribozymes) – Protein synthesis (tRNA and rRNA) 46sanjukaladharan
  47. 47. sanjukaladharan 47 28.10 Base Pairing in Dna: The Watson–Crick Model • In 1953 Watson and Crick noted that DNA consists of 2 polynucleotide strands, running in opposite directions and coiled around each other in a double helix • Strands are held together by hydrogen bonds between specific pairs of bases • Adenine (A) and thymine (T) grade stiff hydrogen bonds to each other but not to C or Chiliad • (Yard) and cytosine (C) form strong hydrogen bonds to each other only not to A or T
  48. 48. sanjukaladharan 48 The Difference in the Strands • The strands of DNA are complementary because of H- bonding • Whenever a Thousand occurs in one strand, a C occurs opposite it in the other strand • When an A occurs in one strand, a T occurs in the other
  49. 49. 49sanjukaladharan
  50. l. Chief Structure of Nucleic Acids • The primary structure of a nucleic acrid is the nucleotide sequence • The nucleotides in nucleic acids are joined by phosphodiester bonds • The iii'-OH grouping of the carbohydrate in one nucleotide forms an ester bail to the phosphate grouping on the 5'-carbon of the carbohydrate of the next nucleotide 50sanjukaladharan
  51. 51. sanjukaladharan 51 Generalized Structure of DNA
  52. 52. Reading Primary Structure • A nucleic acid polymer has a free five'- phosphate group at i end and a free 3'-OH group at the other end • The sequence is read from the free five'-finish using the messages of the bases • This example reads 5'—A—C—Grand—T—3' 52sanjukaladharan
  53. 53. The strands of DNA are antiparallel The strands are costless There are Hydrogen bond forces At that place are base stacking interactions There are x base pairs per turn Properties of a DNA double helix 53sanjukaladharan
  54. 54. Untwisted it looks like this: • The sides of the ladder are: P = phosphate Southward = sugar molecule • The steps of the ladder are C, G, T, A = nitrogenous bases (Nitrogenous means containing the element nitrogen.) A = Adenine T = Thymine A always pairs with T in Dna C = Cytosine G = Guanine C always pairs with G in DNANucleotide (Apples are Tasty) (Cookies are Proficient) 54sanjukaladharan
  55. 55. Secondary Structure: DNA Double Helix • In DNA there are two strands of nucleotides that air current together in a double helix - the strands run in reverse directions - the bases are are arranged in step-like pairs - the base pairs are held together past hydrogen bonding • The pairing of the bases from the ii strands is very specific • The complimentary base of operations pairs are A-T and G-C - two hydrogen bonds form betwixt A and T - three hydrogen bonds form between Grand and C • Each pair consists of a purine and a pyrimidine, so they are the same width, keeping the two strands at equal distances from each other 55sanjukaladharan
  56. 56. sanjukaladharan 56
  57. 57. sanjukaladharan 57
  58. 58. sanjukaladharan 58
  59. 59. Ribonucleic Acid (RNA) • RNA is much more abundant than Dna • There are several important differences between RNA and Dna: - the pentose saccharide in RNA is ribose, in DNA it's deoxyribose - in RNA, uracil replaces the base thymine (U pairs with A) - RNA is single stranded while DNA is double stranded - RNA molecules are much smaller than DNA molecules • There are iii main types of RNA: - ribosomal (rRNA), messenger (mRNA) and transfer (tRNA) 59sanjukaladharan
  60. 60. Types of RNA 60sanjukaladharan
  61. 61. sanjukaladharan 61 Messenger RNA (mRNA) • Its sequence is copied from genetic DNA • It travels to ribsosomes, small granular particles in the cytoplasm of a cell where protein synthesis takes identify
  62. 62. sanjukaladharan 62 Ribosomal RNA (rRNA) • Ribosomes are a complex of proteins and rRNA • The synthesis of proteins from amino acids and ATP occurs in the ribosome • The rRNA provides both structure and catalysis
  63. 63. sanjukaladharan 63 Transfer RNA (tRNA) • Transports amino acids to the ribosomes where they are joined together to brand proteins • At that place is a specific tRNA for each amino acrid • Recognition of the tRNA at the anti- codon communicates which amino acid is attached
  64. 64. Transfer RNA • Transfer RNA translates the genetic code from the messenger RNA and brings specific amino acids to the ribosome for protein synthesis • Each amino acrid is recognized by i or more specific tRNA • tRNA has a tertiary structure that is L-shaped - i end attaches to the amino acid and the other binds to the mRNA by a 3-base free sequence 64sanjukaladharan
  65. 65. Ribosomal RNA and Messenger RNA • Ribosomes are the sites of protein synthesis - they consist of ribosomal Dna (65%) and proteins (35%) - they have two subunits, a large one and a minor 1 • Messenger RNA carries the genetic code to the ribosomes - they are strands of RNA that are complementary to the DNA of the cistron for the protein to be synthesized 65sanjukaladharan
  66. 66. Proteins sanjukaladharan 66
  67. 67. Proteins Come In Many Varieties! • Proteins include a diversity of structures, resulting in a wide range of functions • Proteins account for more than than l% of the dry mass of most cells • Protein functions include structural support, storage, send, cellular communications, movement, and defense force confronting foreign substances 67sanjukaladharan
  68. 68. Enzymatic 68 Enzymatic proteins Enzyme Case: Digestive enzymes catalyze the hydrolysis of bonds in food molecules. Office: Selective acceleration of chemical reactions sanjukaladharan
  69. 69. Storage 69 Storage proteins Ovalbumin Amino acids for embryo Function: Storage of amino acids Examples: Casein, the protein of milk, is the major source of amino acids for baby mammals. Plants accept storage proteins in their seeds. Ovalbumin is the protein of egg white, used as an amino acid source for the developing embryo. sanjukaladharan
  70. seventy. Defensive seventy Defensive proteins Virus Antibodies Bacterium Function: Protection against disease Instance: Antibodies inactivate and help destroy viruses and bacteria. sanjukaladharan
  71. 71. Transport 71 Transport proteins Transport protein Cell membrane Function: Ship of substances Examples: Hemoglobin, the iron-containing protein of vertebrate claret, transports oxygen from the lungs to other parts of the body. Other proteins transport molecules beyond cell membranes. sanjukaladharan
  72. 72. Hormonal proteins Contractile and motor proteins Receptor proteins Structural proteins Example: Insulin, a hormone secreted by the pancreas, causes other tissues to take upwards glucose, thus regulating blood saccharide concentration. Role: Coordination of an organism's activities Normal blood sugar Loftier blood carbohydrate Insulin secreted Examples: Motor proteins are responsible for the undulations of cilia and flagella. Actin and myosin proteins are responsible for the wrinkle of muscles. Role: Movement Muscle tissue Actin Myosin 30 µm Connective tissue threescore µm Collagen Examples: Keratin is the protein of hair, horns, feathers, and other skin appendages. Insects and spiders utilise silk fibers to make their cocoons and webs, respectively. Collagen and elastin proteins provide a fibrous framework in animal connective tissues. Function: Support Signaling molecules Receptor protein Example: Receptors congenital into the membrane of a nerve prison cell discover signaling molecules released by other nerve cells. Office: Response of cell to chemic stimuli 72sanjukaladharan
  73. 73. More About Enzymes 73 • Enzymes are a type of protein that acts as a goad to speed upward chemical reactions • Enzymes tin perform their functions repeatedly, functioning equally workhorses that deport out the processes of life sanjukaladharan
  74. 74. Amino Acids: Yet Another Monomer • Amino acids are organic molecules with carboxyl and amino groups • Amino acids differ in their properties due to differing side chains, chosen R groups 74 Side chain (R group) Amino group Carboxyl grouping α carbon sanjukaladharan
  75. 75. sanjukaladharan 75
  76. 76. Polypeptides • Polypeptides are unbranched polymers built from the same set of 20 amino acids • A protein is a biologically functional molecule that consists of one or more polypeptides 76sanjukaladharan
  77. 77. npolar side chains; hydrophobic Side chain Glycine (Gly or G) Alanine (Ala or A) Valine (Val or Five) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or K) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P) Hydrophobic: Therefore retreat from water! 77sanjukaladharan
  78. 78. 78 Hydrophilic: Therefore Are Attracted to Water sanjukaladharan
  79. 79. 79 Hydrophilic: But Electrically Charged! sanjukaladharan
  80. 80. Peptide Bonds • Amino acids are linked by peptide bonds • A polypeptide is a polymer of amino acids • Polypeptides range in length from a few to more than a m monomers (Yikes!) • Each polypeptide has a unique linear sequence of amino acids, with a carboxyl cease (C-terminus) and an amino end (N-terminus) 80sanjukaladharan
  81. 81. Peptide Bonds 81sanjukaladharan
  82. 82. Peptide Bonds 82sanjukaladharan
  83. 83. Protein Construction & Function • At beginning, all we have is a string of AA's bound with peptide bonds. • One time the string of AA'southward interacts with itself and its environment (often aqueous), then we accept a functional protein that consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape • The sequence of amino acids determines a poly peptide'south three-dimensional construction • A protein's construction determines its function 83sanjukaladharan
  84. 84. Protein Construction: iv Levels • Master structure consists of its unique sequence of amino acids • Secondary structure, plant in near proteins, consists of coils and folds in the polypeptide chain • Tertiary structure is adamant by interactions amid diverse side chains (R groups) • Quaternary structure results when a protein consists of multiple polypeptide bondage 84sanjukaladharan
  85. 85. Primary Structure • Principal construction, the sequence of amino acids in a protein, is like the order of messages in a long word • Primary structure is determined by inherited genetic information 85sanjukaladharan
  86. 86. Secondary Structure • The coils and folds of secondary structure consequence from hydrogen bonds betwixt repeating constituents of the polypeptide courage • Typical secondary structures are a coil called an α helix and a folded structure called a β pleated sail 86sanjukaladharan
  87. 87. Secondary Structure 87sanjukaladharan
  88. 88. 3rd Construction • Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents • These interactions betwixt R groups include bodily ionic bonds and strong covalent bonds called disulfide bridges which may reinforce the protein's structure. • IMFs such as London dispersion forces (LDFs a.k.a. and van der Waals interactions), hydrogen bonds (IMFs), and hydrophobic interactions (IMFs) may affect the poly peptide'south construction 88sanjukaladharan
  89. 89. Tertiary Structure 89sanjukaladharan
  90. xc. Quaternary Structure • Quaternary structure results when two or more polypeptide chains form one macromolecule • Collagen is a gristly poly peptide consisting of three polypeptides coiled similar a rope 90sanjukaladharan
  91. 91. Quaternary Structure • Hemoglobin is a globular protein consisting of 4 polypeptides: two alpha and ii beta chains 91sanjukaladharan
  92. 92. Four Levels of Poly peptide Construction Revisited 92sanjukaladharan
  93. 93. Sickle-Cell Disease: A modify in Primary Structure • A slight modify in primary structure can affect a protein's structure and ability to role • Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the poly peptide hemoglobin 93 "Normal" Red Claret Cells sanjukaladharan
  94. 94. Sickle-Jail cell Illness: A change in Primary Structure • A slight change in primary structure can bear on a protein's structure and ability to function • Sickle-cell illness, an inherited blood disorder, results from a unmarried amino acid substitution in the protein hemoglobin 94sanjukaladharan
  95. 95. What Determines Poly peptide Structure? • In add-on to principal structure, physical and chemical weather can affect structure • Alterations in pH, table salt concentration, temperature, or other environmental factors can cause a protein to unravel • This loss of a protein'southward native construction is chosen denaturation • A denatured protein is biologically inactive 95sanjukaladharan
  96. 96. Denature: Break Bonds or Disrupt IMFs 96sanjukaladharan
  97. 97. carbohydrates sanjukaladharan 97
  98. 98. Carbohydrates serve as fuel and building material • Carbohydrates include sugars and the polymers of sugars • The simplest carbohydrates are monosaccharides, or unmarried sugars • Saccharide macromolecules are polysaccharides, polymers equanimous of many sugar building blocks © 2011 Pearson Education, Inc. 98sanjukaladharan
  99. 99. Sugars • Monosaccharides have molecular formulas that are usually multiples of CH2O • Glucose (C6H12O6) is the most common monosaccharide • Monosaccharides are classified by – The location of the carbonyl group (as aldose or ketose) – The number of carbons in the carbon skeleton © 2011 Pearson Education, Inc. 99sanjukaladharan
  100. 100. Effigy 5.3 Aldoses (Aldehyde Sugars) Ketoses (Ketone Sugars) Glyceraldehyde Trioses: 3-carbon sugars (C3H6O3) Dihydroxyacetone Pentoses: 5-carbon sugars (C5H10O5) Hexoses: vi-carbon sugars (C6H12O6) Ribose Ribulose Glucose Galactose Fructose 100sanjukaladharan
  101. 101. Figure v.3a Aldose (Aldehyde Saccharide) Ketose (Ketone Sugar) Glyceraldehyde Trioses: iii-carbon sugars (C3H6O3) Dihydroxyacetone 101sanjukaladharan
  102. 102. Figure 5.3b Pentoses: 5-carbon sugars (C5H10O5) Ribose Ribulose Aldose (Aldehyde Carbohydrate) Ketose (Ketone Sugar) 102sanjukaladharan
  103. 103. Effigy v.3c Aldose (Aldehyde Sugar) Ketose (Ketone Sugar) Hexoses: 6-carbon sugars (C6H12O6) Glucose Galactose Fructose 103sanjukaladharan
  104. 104. • Though oftentimes drawn equally linear skeletons, in aqueous solutions many sugars form rings • Monosaccharides serve as a major fuel for cells and equally raw material for building molecules © 2011 Pearson Instruction, Inc. 104sanjukaladharan
  105. 105. Figure v.4 (a) Linear and band forms (b) Abbreviated ring structure 1 2 3 iv 5 half-dozen half dozen 5 4 3 2 i 1 2 3 iv v 6 one 23 four 5 half-dozen 105sanjukaladharan
  106. 106. • A disaccharide is formed when a dehydration reaction joins two monosaccharides • This covalent bail is called a glycosidic linkage © 2011 Pearson Teaching, Inc. 106sanjukaladharan
  107. 107. Figure 5.v (a) Dehydration reaction in the synthesis of maltose (b) Dehydration reaction in the synthesis of sucrose Glucose Glucose Glucose Maltose Fructose Sucrose 1–four glycosidic linkage one–2 glycosidic linkage 1 4 1 2 107sanjukaladharan
  108. 108. Polysaccharides • Polysaccharides, the polymers of sugars, take storage and structural roles • The structure and part of a polysaccharide are determined by its sugar monomers and the positions of glycosidic linkages © 2011 Pearson Education, Inc. 108sanjukaladharan
  109. 109. Storage Polysaccharides • Starch, a storage polysaccharide of plants, consists entirely of glucose monomers • Plants store surplus starch equally granules inside chloroplasts and other plastids • The simplest grade of starch is amylose © 2011 Pearson Education, Inc. 109sanjukaladharan
  110. 110. Figure 5.6 (a) Starch: a plant polysaccharide (b) Glycogen: an creature polysaccharide Chloroplast Starch granules Mitochondria Glycogen granules Amylopectin Amylose Glycogen 1 µm 0.5 µm 110sanjukaladharan
  111. 111. Figure v.6a Chloroplast Starch granules one µm 111sanjukaladharan
  112. 112. • Glycogen is a storage polysaccharide in animals • Humans and other vertebrates store glycogen mainly in liver and muscle cells © 2011 Pearson Education, Inc. 112sanjukaladharan
  113. 113. Figure five.6b Mitochondria Glycogen granules 0.5 µm 113sanjukaladharan
  114. 114. Structural Polysaccharides • The polysaccharide cellulose is a major component of the tough wall of plant cells • Like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ • The difference is based on ii ring forms for glucose: alpha (α) and beta (β) © 2011 Pearson Education, Inc. 114sanjukaladharan
  115. 115. Figure 5.7 (a) α and β glucose band structures (b) Starch: 1–4 linkage of α glucose monomers (c) Cellulose: 1–4 linkage of β glucose monomers α Glucose β Glucose iv 1 4 1 41 41 115sanjukaladharan
  116. 116. Figure five.7a (a) α and β glucose ring structures α Glucose β Glucose 4 1 4 1 116sanjukaladharan
  117. 117. Figure 5.7b (b) Starch: 1–4 linkage of α glucose monomers (c) Cellulose: 1–four linkage of β glucose monomers 41 41 117sanjukaladharan
  118. 118. © 2011 Pearson Education, Inc. • Polymers with α glucose are helical • Polymers with β glucose are directly • In straight structures, H atoms on one strand can bail with OH groups on other strands • Parallel cellulose molecules held together this way are grouped into microfibrils, which course potent building materials for plants 118sanjukaladharan
  119. 119. Cell wall Microfibril Cellulose microfibrils in a plant prison cell wall Cellulose molecules β Glucose monomer 10 µm 0.5 µm Figure v.8 119sanjukaladharan
  120. 120. • Enzymes that digest starch by hydrolyzing α linkages tin't hydrolyze β linkages in cellulose • Cellulose in human nutrient passes through the digestive tract as insoluble fiber • Some microbes utilize enzymes to digest cellulose • Many herbivores, from cows to termites, accept symbiotic relationships with these microbes © 2011 Pearson Education, Inc. 120sanjukaladharan
  121. 121. • Chitin, another structural polysaccharide, is found in the exoskeleton of arthropods • Chitin also provides structural support for the jail cell walls of many fungi © 2011 Pearson Education, Inc. 121sanjukaladharan
  122. 122. LIPIDS sanjukaladharan 122
  123. 123. sanjukaladharan 123
  124. 124. Lipids are a diverse group of hydrophobic molecules • Lipids are the one class of large biological molecules that practise not grade polymers • The unifying feature of lipids is having niggling or no affinity for water • Lipids are hydrophobic considering they consist mostly of hydrocarbons, which course nonpolar covalent bonds • The near biologically of import lipids are fats, phospholipids, and steroids © 2011 Pearson Education, Inc. 124sanjukaladharan
  125. 125. Fats • Fats are constructed from two types of smaller molecules: glycerol and fatty acids • Glycerol is a three-carbon booze with a hydroxyl group attached to each carbon • A fat acid consists of a carboxyl grouping attached to a long carbon skeleton © 2011 Pearson Education, Inc. 125sanjukaladharan
  126. 126. Figure 5.10 (a) One of 3 dehydration reactions in the synthesis of a fatty (b) Fat molecule (triacylglycerol) Fatty acrid (in this instance, palmitic acid) Glycerol Ester linkage 126sanjukaladharan
  127. 127. Figure 5.10a (a) One of three dehydration reactions in the synthesis of a fatty Fat acid (in this instance, palmitic acid) Glycerol 127sanjukaladharan
  128. 128. © 2011 Pearson Education, Inc. • Fats separate from h2o considering water molecules grade hydrogen bonds with each other and exclude the fats • In a fat, three fat acids are joined to glycerol by an ester linkage, creating a triacylglycerol, or triglyceride 128sanjukaladharan
  129. 129. Figure v.10b (b) Fat molecule (triacylglycerol) Ester linkage 129sanjukaladharan
  130. 130. • Fat acids vary in length (number of carbons) and in the number and locations of double bonds • Saturated fat acids take the maximum number of hydrogen atoms possible and no double bonds • Unsaturated fatty acids take one or more double bonds © 2011 Pearson Education, Inc. 130sanjukaladharan
  131. 131. © 2011 Pearson Didactics, Inc. Blitheness: Fats Right-click slide / select "Play" 131sanjukaladharan
  132. 132. Figure 5.11 (a) Saturated fat (b) Unsaturated fat Structural formula of a saturated fatty molecule Space-filling model of stearic acid, a saturated fat acid Structural formula of an unsaturated fat molecule Space-filling model of oleic acid, an unsaturated fat acrid Cis double bond causes bending. 132sanjukaladharan
  133. 133. (a) Saturated fat Structural formula of a saturated fat molecule Space-filling model of stearic acid, a saturated fatty acrid Effigy five.11a 133sanjukaladharan
  134. 134. Figure 5.11b (b) Unsaturated fat Structural formula of an unsaturated fatty molecule Space-filling model of oleic acid, an unsaturated fat acid Cis double bond causes angle. 134sanjukaladharan
  135. 135. • Fats made from saturated fatty acids are called saturated fats, and are solid at room temperature • Most animal fats are saturated • Fats made from unsaturated fatty acids are called unsaturated fats or oils, and are liquid at room temperature • Found fats and fish fats are usually unsaturated © 2011 Pearson Education, Inc. 135sanjukaladharan
  136. 136. • A nutrition rich in saturated fats may contribute to cardiovascular disease through plaque deposits • Hydrogenation is the process of converting unsaturated fats to saturated fats by adding hydrogen • Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds • These trans fats may contribute more than than saturated fats to cardiovascular disease © 2011 Pearson Educational activity, Inc. 136sanjukaladharan
  137. 137. • Sure unsaturated fat acids are not synthesized in the human body • These must be supplied in the nutrition • These essential fatty acids include the omega-three fatty acids, required for normal growth, and idea to provide protection against cardiovascular disease © 2011 Pearson Education, Inc. 137sanjukaladharan
  138. 138. • The major function of fats is free energy storage • Humans and other mammals store their fat in adipose cells • Adipose tissue also cushions vital organs and insulates the body © 2011 Pearson Education, Inc. 138sanjukaladharan
  139. 139. Phospholipids • In a phospholipid, two fatty acids and a phosphate group are attached to glycerol • The 2 fat acid tails are hydrophobic, just the phosphate group and its attachments form a hydrophilic head © 2011 Pearson Education, Inc. 139sanjukaladharan
  140. 140. Figure 5.12 Choline Phosphate Glycerol Fatty acids Hydrophilic head Hydrophobic tails (c) Phospholipid symbo(b) Space-filling modela) Structural formula HydrophilicheadHydrophobictails 140sanjukaladharan
  141. 141. Choline Phosphate Glycerol Fatty acids (b) Space-filling model(a) Structural formula HydrophilicheadHydrophobictails Figure 5.12a 141sanjukaladharan
  142. 142. • When phospholipids are added to water, they self- assemble into a bilayer, with the hydrophobic tails pointing toward the interior • The structure of phospholipids results in a bilayer arrangement institute in jail cell membranes • Phospholipids are the major component of all cell membranes © 2011 Pearson Educational activity, Inc. 142sanjukaladharan
  143. 143. Figure 5.13 Hydrophilic head Hydrophobic tail WATER WATER 143sanjukaladharan
  144. 144. Steroids • Steroids are lipids characterized by a carbon skeleton consisting of four fused rings • Cholesterol, an important steroid, is a component in animal prison cell membranes • Although cholesterol is essential in animals, high levels in the blood may contribute to cardiovascular illness © 2011 Pearson Didactics, Inc. 144sanjukaladharan
  145. 145. Figure 5.fourteen 145sanjukaladharan
  146. 146. Macromolecular assembly (MA) • The term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologicnanoparticles cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric molecules. • They are generally of more than than one of these types, and the mixtures are defined spatially (i.e., with regard to their chemical shape), and with regard to their underlying chemic composition and structure. 146sanjukaladharan
  147. 147. Figure 13.13 Annotation: South or Svedberg units are not additive A ribosome is equanimous of structures called the large and modest subunits Each subunit is formed from the assembly of Proteins + rRNA Bacterial Ribosomes (and mitochondrial/chloroplast) 147sanjukaladharan
  148. 148. Figure 13.13 The 40S and 60S subunits are assembled in the nucleolus And so exported to the cytoplasm Formed in the cytoplasm during translation Eukaryotic Ribosomes 148sanjukaladharan
  149. 149. Ribosomes comprise three discrete sites: Peptidyl site (P site) Aminoacyl site (A site) Get out site (Eastward site) 149sanjukaladharan
  150. 150. Release factors Initiator tRNA Three Stages: Initiation Elongation Termination 150sanjukaladharan
  151. 151. Give thanks YOU sanjukaladharan 151

  • This lesson will deal with poly peptide and nucleic acids. Emphasize yet again that within the molecule, the intramolecular forces are covalent bonds, just the intermolecular forces (IMFs) betwixt molecules will vary due to the polarity of the molecule as a whole.
  • Enquire students what they already know about proteins and protein synthesis. Hopefully, they retrieve a few things from Biology I.
  • Emphasize the specificity of enzymes. Also emphasize the catalytic nature of enzymes and that they part best in a unique set of pH and temperature conditions. Why is that? It is due to the shape of the enzyme molecule. That shape is held in place by IMFs and/or covalent or ionic bonding. Changes in pH or temperature often disrupt the electrostatic forces that are responsible for an enzyme'due south specific shape.
  • Enquire students to identify other food sources that are proteins. One of my favorite quotes ever is from Bob Harper, a personal trainer from The Biggest Loser. Just put, "If the food in question had a mother, and so it's a protein!"
  • Enquire students which torso system utilizes these types of proteins.
  • Ask which torso arrangement utilizes hemoglobin.
  • Figure three.16b An overview of poly peptide functions (part 7)
  • This is a perfect time to bring out the "water noodle" enzyme models. You can extend this portion of the lesson to include competitive inhibition, etc.
  • In that location are 23 amino acids (aa'south) only merely 20 are biologically active.
  • Enquire, how many peptide bonds are formed. Enquire how many amino acids are in this polypeptide. Additionally, emphasize the arrangement of the aa'south in this diagram. If one of the aa's is "flipped" along the horizontal centrality, it's amine group no longer aligns with the neighboring aa's carboxylic acid group, thus no dehydration reaction can occur.
  • Absolutely no need to memorize these, just there is a need to recognize WHY these retreat from water. Point out that these "R" groups are very nonpolar as evidenced past the "hydrocarbonish" or CHX nature of the elements involved in the R groups.
  • Admittedly no demand to memorize these, but emphasize that while these R groups also wait "hydrocarbonish", that there are unpaired electrons left off this diagram. Each N, O or Due south atom has unshared electron pairs that make them polar and h2o soluble.
  • Once again, no need to memorize these but students should know that ammonia (NH3) is a weak base from Chemistry I. Remove an H from ammonia and y'all take its "cousin" the amine grouping which is likewise basic.
  • Emphasize that the peptide bond forms equally a effect of a dehydration synthesis reaction.
  • Now is the time to explain that a string of aa'southward is a polypeptide and Non notwithstanding a protein. The protein forms in one case the secondary, tertiary and quaternary structures are established and that is commonly facilitated in an aqueous environment. Also emphasize that "conformation" is the "large people" give-and-take for shape and that if the conformation changes, the part of the poly peptide is afflicted.
  • Go on it simple. Explain to students that when they were nearly 3 years old, they would sing the alphabet song to anyone that would listen! They had no idea that one day they'd use that to spell or that they would use it to read, or write sentences, or paragraphs or research papers!
    As well, remind them yet once again that they have some prior noesis regarding Dna and the process of poly peptide synthesis.
  • Emphasize withal again that a H-bond is Not a bonded H! Information technology's an IMF, not a covalent bond, simply rather an electrostatic strength. H-bonds are fragile and hands interrupted by pH or temperature changes.
  • Linus Pauling is my favorite scientist, so I'd accept to share that he won his first Nobel Prize in Chemistry in 1954  "for his research into the nature of the chemical bail and its application to the elucidation of the structure of complex substances". Those complex substances are proteins and he figured out the  helix and a folded structure chosen a  pleated sheet! Students may know that the electronegativity scale they learned in Chemical science I is the "Pauling Electronegativity Scale". But, they may non know that he was hot on the heels of chirapsia Watson & Crick to the "discovery" of the construction of DNA OR that he also won a Nobel Prize for Peace. Whew!
  • Here we go once more, the second bullet refers to actual chemical bonds—the sharing of a pair of electrons. The 3rd bullet refers to intermolecular forces (IMFs) with LDFs that the biological science books often refer to every bit van der Waals forces or interactions. H-bonds are a special example of dipole-dipole interactions. While none of these distinctions will be asked on the AP Biological science exam, they certainly will on the AP Chemistry examination and should be taught in Chem I besides. It's not surprising that students are confused since the vocabulary is so different from book to book! Ugh!
  • Revisit the "curly pilus" example for disulfide bridges. Folks with curly hair have more than disulfide bridges and we oft use estrus to alter them 1.Utilise a hair dryer-brush-mechanically pull on the hair while applying heat to disrupt the S-S bridges. ii. Flat irons on dry pilus 3. "Perms"—A basic solution that reeks of ammonia (a base, thus a pH rather than thermal approach) is applied to hair that has been wound onto skinny curlers and left to sit for nigh 20 minutes to allow Southward-S to course.
  • Emphasize that Quaternary structure involves a collection of polypeptides brought together into a new conformation.
  • The classic instance!
  • A nice visual summary!
  • A perfect practical case of how a change in protein structure affects function. Be sensitive to the fact that y'all may accept a student that suffers from sickle-prison cell disease.
  • The sickled cells cannot motion the blood vessels as effectively and can obstruct capillaries and restrict blood menstruum to an organ, resulting in pain, necrosis and frequently organ harm. Ask if students studied the connectedness between sickle-cell trait and malaria in Biological science I.
  • Enquire how EACH of the items mentioned could disrupt protein structure.
  • This concept is an energy concept likewise. If thermal energy is added, the molecules vibrate more vigorously. At some signal the electrostatic attractions (H-bonds) are overcome and "let go".
    When students write costless-responses, make sure they define terms they use within their writing. "A change in temperature denatures a poly peptide since the H-bonds (or IMFs) are disrupted (or overcome, or altered, or anything else that implies the structure is cleaved downwardly)." Lots of means to wordsmith the response correctly!
  • Figure 5.3 The construction and classification of some monosaccharides.
  • Figure 5.three The construction and classification of some monosaccharides.
  • Effigy 5.3 The structure and classification of some monosaccharides.
  • Figure 5.3 The structure and classification of some monosaccharides.
  • Figure v.iv Linear and ring forms of glucose.
  • Figure 5.5 Examples of disaccharide synthesis.
  • Figure 5.half dozen Storage polysaccharides of plants and animals.
  • Figure five.six Storage polysaccharides of plants and animals.
  • Figure 5.6 Storage polysaccharides of plants and animals.
  • Figure 5.seven Starch and cellulose structures.
  • Figure 5.7 Starch and cellulose structures.
  • Effigy v.7 Starch and cellulose structures.
  • Figure 5.8 The system of cellulose in plant cell walls.
  • Figure five.10 The synthesis and structure of a fat, or triacylglycerol.
  • Figure 5.ten The synthesis and structure of a fat, or triacylglycerol.
  • Figure five.x The synthesis and structure of a fat, or triacylglycerol.
  • Figure 5.11 Saturated and unsaturated fats and fatty acids.
  • Figure v.11 Saturated and unsaturated fats and fatty acids.
  • Figure 5.11 Saturated and unsaturated fats and fatty acids.
  • Figure 5.12 The structure of a phospholipid.
  • Figure 5.12 The structure of a phospholipid.
  • Figure 5.13 Bilayer structure formed past self-associates of phospholipids in an aqueous environs.
  • For the Cell Biology Video Space Filling Model of Cholesterol, go to Animation and Video Files.
    For the Cell Biological science Video Stick Model of Cholesterol, go to Animation and Video Files.
  • Figure 5.14 Cholesterol, a steroid.
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