Term
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Definition
| the spatial arrangement of atoms in a protein or any part of a protein |
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Term
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Definition
| proteins in any of their functional, folded conformations |
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Term
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Definition
| the tendency to maintain a native protein structure conformation |
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Term
| What type of weak interaction predominates when it comes to protein stability? |
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Definition
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Term
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Definition
| a highly structured shell of water around the molecule that results from the optimal arrangement of hydrogen bonds when water surrounds a hydrophobic molecule |
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Term
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Definition
| any chosen segment of a polypeptide chain; the local spatial arrangement of a polypeptide's main chain atoms without regard to the positioning of its side chains or its relationship to other segments |
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Term
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Definition
| the arrangement of several segments side by side all of which are in the beta conformation |
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Term
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Definition
| common turns that connect the ends of two adjacent segments of an antiparallel beta sheet |
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Term
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Definition
| the overall three-dimensional arrangement of all atoms in a protein |
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Term
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Definition
| the arrangement of protein subunits in three-dimensional complexes |
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Term
| 2 major groups into which proteins can be classified when it comes to higher levels of structure |
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Definition
1. fibrous proteins (polypeptide chains arranged in long strands or sheets)
2. globular proteins (polypeptide chains folded into a spherical or globular shape) |
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Term
| 4 rules pertaining to common protein folding patterns |
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Definition
1. hydrophobic interactions make a large contribution to the stability of protein structures
2. where they occur together in a protein, alpha helices & beta sheets are found in different structural layers
3. segments adjacent to each other in the amino acid sequence are stacked adjacent to each other in the folded structure
4. the beta conformation is most stable when the individual segments are twisted slightly in a right-handed sense |
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Term
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Definition
| the particularly stable & common motif where a series of beta-alpha-beta loops are arranged so that the beta strands form a barrel |
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Term
| 4 classes of protein structure at the highest level of classification |
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Definition
1. all alpha
2. all beta
3. alpha/beta
4. alpha + beta |
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Term
| the top 2 levels of organization that are purely structural |
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Definition
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Term
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Definition
| proteins with significant similarity in primary structure and/or with similar tertiary structure & function |
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Term
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Definition
| when two or more families with little similarity in amino acid sequence make use of the same major structural motif & have functional similarities |
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Term
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Definition
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Term
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Definition
| a multimer with just a few subunits |
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Term
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Definition
| the repeating structural unit in a multimeric protein, whether a single subunit or a group of subunits |
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Term
| Do intrinsically disordered proteins have properties that are similar to or distinct from classical structured proteins? |
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Definition
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Term
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Definition
| the continual maintenance of the active set of cellular proteins required under a given set of conditions |
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Term
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Definition
| a loss of three-dimensional structure sufficient to cause loss of function |
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Term
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Definition
| proteins that interact with partially folded or improperly folded polypeptides to facilitate correct folding pathways or providing microenvironments in which folding can occur; folding for many proteins requires them |
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Term
| 2 major families of chaperones |
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Definition
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Term
| protein disulfide isomerase (PDI) |
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Definition
| a widely distributed enzyme that catalyzes the interchange (shuffling) of disulfide bonds until the bonds of the native conformation are formed |
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Term
| peptide prolyl cis-trans isomerase (PPI) |
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Definition
| catalyzes the interconversion of the cis & trans isomers of Pro residue peptide bonds |
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