[Hydration of the left spiral of the poly-L-proline type. Study by the Monte Carlo method].
The paper exhibits results of hydration shell Monte Carlo calculations in poly-L-proline II and extended helix conformation and in alpha-helical and beta-structural conformations for comparison. It was found that left-handed helix of poly-L-proline II type as well as epsilon-helix are characterized by very favorable hydration. Therefore this conformation has preference as compared to other standard conformations of the main polypeptide chain. This determined inevitability of cold denaturation of protein.
Aĭzenkhaber
F
F
Central Institute of Molecular Biology, Berlin-Buch, FRG.
Adzhubeĭ
A A
AA
Aĭzenmenger
F
F
Esipova
N G
NG
D000595:Amino Acid Sequence; D003080:Cold Temperature; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D014867:Water / Q000737:chemistry*
D010455:Peptides; D014867:Water; C011083:polyproline
Gidratsiia levoĭ spirali tipa poli-L-prolin. II. Issledovanie metodom Monte Karlo.