[Molecular dynamics of bending fluctuations in the protein secondary structures].
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.
Shaĭtan
K V
KV
Lomonosov Moscow State University, Vorob'evy Gory, Moscow, 119899 Russia.
Mikhaĭliuk
M G
MG
Leont'ev
K M
KM
Saraĭkin
S S
SS
Beliakov
A A
AA
D001426:Bacterial Proteins; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011107:Polylysine / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry
D001426:Bacterial Proteins; D008164:Luminescent Proteins; D009211:Myoglobin; D010455:Peptides; D011506:Proteins; D049452:Green Fluorescent Proteins; D011107:Polylysine; C011080:polyglycine; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease
Molekuliarnaia dinamika izgibnykh fluktuatsiĭ élementov vtorichnoĭ struktury belkov.