Journal
JOURNAL OF CHEMICAL PHYSICS
Volume 130, Issue 12, Pages -Publisher
AMER INST PHYSICS
DOI: 10.1063/1.3050103
Keywords
biochemistry; molecular biophysics; molecular configurations; proteins
Funding
- Ministry of Science and Higher Education in Poland [NN202085233]
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We incorporate hydrodynamic interactions (HIs) in a coarse-grained and structure-based model of proteins by employing the Rotne-Prager hydrodynamic tensor. We study several small proteins and demonstrate that HIs facilitate folding. We also study HIV-1 protease and show that HIs make the flap closing dynamics faster. The HIs are found to affect time correlation functions in the vicinity of the native state even though they have no impact on same time characteristics of the structure fluctuations around the native state.
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