Protein Structural Flexibility: Molecular Motions

Richard H Henchman, School of Chemistry, UK
J Andrew McCammon, Howard Hughes Medical Institute, USA

Published online: September 2005

DOI: 10.1038/npg.els.0003012

Protein molecules are intrinsically flexible and typically undergo a wide variety of motions at normal temperatures. The flexibility and dynamics of proteins have been harnessed by evolution for a wide variety of their activities, ranging from ligand binding to regulation of function.

Keywords: protein dynamics; enzyme mechanisms; allostery

Figure 1. The flexible torsion angles in the polypeptide chain. The most flexible (green) are the side-chain torsions represented by , moderate flexibility are and (orange) and restricted flexibility (red) is the peptide bond, .
Figure 2. Schematic representation of the motions involved in an enzyme (orange) catalysed process on a substrate (red). The motion of the enzyme during this reaction can also be harnessed to do work.
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 Further Reading
    Baumeister W and Steven AC (2000) Macromolecular electron microscopy in the era of structural genomics. Trends in Biochemical Science 25: 624–631.
    book Carter CW Jr (ed.) (1997) "Macromolecular crystallography. Part A". Methods in Enzymology 276: 3–700.
    book Carter CW Jr and Sweet RM (eds) (1997) "Macromolecular crystallography. Part B". Methods in Enzymology 277: 3–664.
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Related Sub-Topics:

Protein Structure | Protein Folding, Evolution and Degradation | Biomolecular Interactions | Proteins: Structure, Function, Metabolism | Enzymes: Structure and Action Mechanism
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Article Title: Protein Structural Flexibility: Molecular Motions
 
How to Cite close
Henchman, Richard H, and McCammon, J Andrew(Sep 2005) Protein Structural Flexibility: Molecular Motions. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0003012]