Protein Conformation
| Definition: |
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). |
| Notes: |
IM general; coord NIM with specific protein; peptide conformation = PEPTIDES or specific peptide (IM) + PROTEIN CONFORMATION (NIM); index protein architecture here or under its specifics |
| Previously Indexed: |
Proteins (1966-1971) |
Protein Conformation Categories.
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Protein Structure, Quaternary - The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain). |
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Protein Structure, Secondary - The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation. |
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Protein Structure, Tertiary - The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure. |
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Structural Homology, Protein - The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN. |
Protein Conformation Definitions and Terms
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