Related Experiment Videos
[Molecular dynamics of bending fluctuations in the protein secondary structures]
K V Shaĭtan1, M G Mikhaĭliuk, K M Leont'ev
1Lomonosov Moscow State University, Vorob'evy Gory, Moscow, 119899 Russia.
Biofizika
|June 19, 2002
Abstract:
A comparative study of the dynamics of protein secondary structure elements by the example of alpha-helices of myoglobin, barnase, polylysine, and polyglycine and beta-layers of barnase and GFP was carried out by the methods of molecular dynamics. The effective Young's moduli of both free secondary structure elements and those built in the protein globule were determined. A heterogeneity of the elastic properties of the secondary structure elements was found. The melting of myoglobin alpha-helix in a virtual viscous medium was studied.