[Double and bifurcated hydrogen bonds in alpha-helices of globular proteins].
The statistical analysis of hydrogen bonds distribution in space structures of globular proteins has been done. The parameters of H-bonds in the different secondary structures of globular proteins were collected. In alpha-helices besides the canonical 1-5 H-bonds (the mean length 3 A), 1-4 H-bonds were observed (the mean length 3.2 A). The histograms of length and angular distributions of the bonds are presented. It was found on the basis of quantum chemistry calculations that most H-bonds in alpha-helices are double or bifurcated.
Faĭn
A V
AV
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow, 119991 Russia.
Berezovskiĭ
I N
IN
Chekhov
V O
VO
Ukrainskiĭ
D L
DL
Esipova
N G
NG
D003627:Data Interpretation, Statistical; D030562:Databases, Protein; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D010455:Peptides; D011506:Proteins
Dvoĭnye i vilochkovye vodorodnye sviazi v al'fa-spiraliakh globuliarnykh belkov.