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| Proteins are polymers made out of amino acids connected by peptide bonds. |
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| 2 scondary protein structures |
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alpha-helix, residues separated by 4 positions form hydrogen bonds between their backbone atoms.
adjacent beta-strands form hydrogen bonds between their backbone atoms. |
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| The biological role of proteins is determined by |
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| The biological role of proteins is determined by their three-dimensional shape |
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| The particular shape that a protein adopts is determined by |
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| Protein structures can be divided into three groups: |
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| globular proteins, fibrous proteins, and integral membrane proteins |
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| Most genes in humans code for _________ proteins which generally have a non-repetitive |
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| Most globular proteins share these characteristics: |
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- Hydrophobic amino acids in the interior of the protein
- polar amino acids on the surface.
- amino acid side chains closely packed, thus, fairly rigid molecules.
- Nearly all buried oxygens and nitrogens are participating in hydrogen bonds with other groups within the protein.
- On the surface, these atoms form hydrogen bonds with water. |
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These are characteristics of what type of protein:
highly elongated, function as structural materials (skin, tendons, bones) or have motive functions (muscle).
repetitive amino acids |
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| Why does a diet deficient in vitamin C lead to a weakening of collagen and the disease scurvy |
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| Prolin, in the Gly-Pro- 4-hydroxyproline (Hyp) repeat, is converted to Hyp by the enzyme prolyl hydroxylase which uses vitamin C as a co-factor. Hyp is crucial to the stability of collagen. |
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| Describe Integral membrane proteins |
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| They are embedded within the hydrophobic environment of the membrane thus the residues on the surface of integral membrane proteins are commonly hydrophobic. |
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| Structure containing multiple polypeptide chains. One example being the ribosome which contains many protein chains and structural RNA |
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| proteins need to be soluble in the absence of their binding partners thus |
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| protein surfaces are not covered with hydrophobic amino acids or they would aggregate in the unbound state. For this reason, hydrogen bonding is often very important in stabilizing protein-protein interactions. |
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| describe Multi-domain Proteins |
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| Many proteins contain independently folding domains connected by flexible linkers |
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| __________ are covalent interactions that form between two cysteines. They can be used to stabilize tertiary and quaternary structure. |
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| Disulfide bonds are more stable in an ___________ environment, and therefore are more prevalent in extra-cellular proteins. |
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| Post-translational Modification include |
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Proteolytic processing
Phosphorylation
Methylation
Hydroxylation
Glycosylation |
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| proteins are cleaved after synthesis by proteases to generate the active form of the protein. Ex Insulin |
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| (the addition of a phosphate group to the oxygen of Ser, Thr or Tyr) is often used to activate signaling proteins. Usually there is a conformational change associated with phosphorylation |
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| (the addition of a methyl group to an amino acid, often lysines) is used among other things to regulate the proteins (histones) that package DNA |
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| (the addition of an OH group to a carbon). Such as in the hydroxylation event important to the structure of collagen. |
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| (the addition of carbohydrates to proteins). Membrane proteins are often glycosylated as it stabilizes the proteins interaction with the membrane. |
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| Protein structures are determined using either __________ or ___________. Both techniques are slow and it can take several years to solve the structure of a protein. |
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X-ray crystallography: a crystal of the protein is required
Nuclear Magnetic Resonance: NMR, can only be used on small proteins |
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