Protein Structural Flexibility: Molecular Motions

Abstract

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 χ, moderate flexibility are γ and ϕ (orange) and restricted flexibility (red) is the peptide bond, ω.

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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References

Benkovic SJ and Hammes‐Schiffer S (2003) A perspective on enzyme catalysis. Science 310: 1196–1202.

Echols N, Milburn D and Gerstein M (2003) MolMovDB: analysis and visualization of conformational change and structural flexibility. Nucleic Acids Research 31: 478–482.

Hook SS and Means AR (2001) Ca2+/CaM‐dependent kinases: from activation to function. Annual Review of Pharmacology and Toxicology 41: 471–505.

Kern D and Zuiderweg ERP (2003) The role of dynamics in allosteric regulation. Current Opinions in Structural Biology 13: 748–757.

Karplus M and McCammon JA (2002) Molecular dynamics simulations of biomolecules. Nature Structural Biology 9: 646–652.

Perutz MF, Wilkinson AJ, Paoli M and Dodson GG (1998) The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annual Reviews of Biophysics and Biomolecular Structure 27: 1–34.

Schliwa M and Woehlke G (2003) Molecular motors. Nature 422: 759–765.

Schotte F, Lim M, Jackson TA et al. (2003) Watching a protein as it functions with 150‐ps time‐resolved X‐ray crystallography. Science 300: 1944–1947.

Wright PE and Dyson HJ (1999) Intrinsically unstructured proteins: re‐assessing the protein structure‐function paradigm. Journal of Molecular Biology 293: 321–331.

Further Reading

Baumeister W and Steven AC (2000) Macromolecular electron microscopy in the era of structural genomics. Trends in Biochemical Science 25: 624–631.

Carter CW Jr (ed.) (1997) Macromolecular crystallography. Part A. Methods in Enzymology 276: 3–700.

Carter CW Jr and Sweet RM (eds) (1997) Macromolecular crystallography. Part B. Methods in Enzymology 277: 3–664.

Fersht A (1999) Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding. New York: Freeman.

McCammon JA and Harvey SC (1987) Dynamics of Proteins and Nucleic Acids. Cambridge: Cambridge University Press.

Krishna NR and Berliner LJ (eds.) (1998) Modern Techniques in Protein NMR, (1999) Structure Computation and Dynamics in Protein NMR, (2003) Protein NMR for the Millenium, Biological Magnetic Resonance. New York: Kluwer Academic–Plenum Publications.

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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]