JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 44(2010) N 3 p. 466-472;
E.V. Brazhnikov, A.V. Efimov*

Structure of β-β-Hairpins Closed into Cycles by S-S-Bridges

Institute of Protein Reseach, Russian Academy of Sciences, Puschino, 142290 Russia

*efimov@protres.ru
Received - 2009-09-16; Accepted - 2009-11-05

In the present study, a stereochemical analysis of proteins containing β-β-hairpins closed into cycles by S-S-bridges has been performed. A database of these proteins has been compiled from the Protein Data Bank (total 428 PDB entries). 390 β-β-hairpins closed into cycles by S-S-bridges have been found in non-homologous proteins included into the database. Analysis showed that 118 hairpins contain S-S-bridges formed by cysteins located opposite to each other in the neighboring β-strands. Among them, 110 hairpins are left-turned and 8 β-hairpins are right-turned when viewed from the same side where S-S-bridges are located. In the other group of 272 β-hairpins, the S-S-bridge is formed by two cysteins one of which is located in the β -strand and the other in the loop juxtaposed to the -hairpin at the N- (84% cases) or C-terminus (16% cases). As shown, in most cases the loop-hairpin region closed into a cycle by the S-S-bridge formed a turn of a left-handed superhelix.

proteins, β-strand, β -turn, conformation, stereochemical analysis, handedness



JMB-FOOTER RAS-JOURNALS