Vibrational dynamics of folded proteins: Significance of slow and fast motions in relation to function and stability

Ivet Bahar, Ali Rana Atilgan, Melik C. Demirel, Burak Erman

Research output: Contribution to journalArticlepeer-review

305 Scopus citations

Abstract

A single-parameter harmonic Hamiltonian based on local packing density and contact topology is proposed for studying residue fluctuations in native proteins. The internal energy obeys an equipartition law, and free energy changes result from entropy fluctuations only. Frequency wave-number maps show communication between residues involved in slow and fast modes. Fast modes are strongly localized, resulting from the geometric irregularity of the structure. Comparison with experiments shows that slow and fast modes are associated, respectively, with function and stability. Specifically, domain motions and folding cores of HIV-1 protease are accurately identified.

Original languageEnglish (US)
Pages (from-to)2733-2736
Number of pages4
JournalPhysical review letters
Volume80
Issue number12
DOIs
StatePublished - 1998

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)

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