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18 Cards in this Set
- Front
- Back
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what does the primary structure show? |
Amino acid sequence of the polypeptide chain |
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100 amino acid residues may be combined in how may different ways? |
10^130 |
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What does the secondary structure show? |
The spatial arrangement of the backbone without regard to the side chain Alpha helix or beta sheet |
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What defines structure of Alpha Helix? |
carbonyl C=O of n residue forms H bond with N-H on n+4 residue |
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What defines structure of Beta Sheet? |
H bonds between parallel backbones, chains can run parallel and non-parallel |
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What is collagen? |
Proteins can be fibrous or globular and is most abundant protein in fibrous form in vertebrates. Made up of Gly, Pro, and hydroxy- Pro residues Collagen is a triple helix protein and the triple helix are major stress bearing components of tissue |
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What the nonstandard amino acid and how is it formed? |
Proline side chain is hydroxylated b prolyl hydroxylase and absorbic acid (coenzyme) Hydroxyl group added to proline helps to form stable structure on normal proline
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What happens when lack of vitamin C? |
Scurvy, Collagen cannot form |
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What defines the tertiary structure? |
Folding of the secondary structure, segments are joined by reverse turns usually at surface of the protein |
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How much energy to unfold a single residue from a protein? |
0.4 kj/mol |
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Where are the polar residues located? |
Usually on surface of protein (hydrophillic) |
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Where are the non- polar residues located? |
Usually concealed on inside (hydrophobic) |
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What is myoglobin and what does it do? |
intracellular protein facilitating oxygen transport in vertebrate muscle, contains a heme group (containing iron) which oxygen binds reversibly to |
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What is the function and structure of the heme group? |
it is four nitrogen bound to central iron, Oxygen reversibly binds but CO and NO sometimes do not reversibly bind |
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How do you convert Myoglobin to metmyoglobin? |
Oxidation of Fe (II) to Fe (III) |
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What is the structure and function of hemoglobin? |
heme is due to red colour, contains 4 subunits, 2 alpha and 2 beta, when oxygen binds the structure is altered, major component of erythrocytes, hemoglobin binds bicarbonate and carries it to the lung to get rid of it |
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What does carbonic anhydrase catalyze? |
CO2>bicarbonate |
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How is sickle cell anemia caused? |
hereditary disease caused by the recessive variant of beta chain, Valine 6 instead of Glutamine 6, Val 6 fits in hydrophobic pocket in another hemoglobin molecule creating a long chain instead of individual molecules |
