Premium
Shorter side chains optimize helix–helix packing
Author(s) -
Jiang Sulin,
Vakser Ilya A.
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.03505804
Subject(s) - helix (gastropod) , transmembrane domain , folding (dsp implementation) , crystallography , transmembrane protein , protein folding , side chain , protein structure , collagen helix , chemistry , triple helix , stereochemistry , membrane , biology , biochemistry , engineering , polymer , ecology , receptor , organic chemistry , snail , electrical engineering
Abstract A systematic study of helix–helix packing in a comprehensive database of protein structures revealed that the side chains inside helix–helix interfaces on average are shorter than those in the noninterface parts of the helices. The study follows our earlier study of this effect in transmembrane helices. The results obtained on the entire database of protein structures are consistent with those obtained on the transmembrane helices. The difference in the length of interface and noninterface side chains is small but statistically significant. It indicates that helices, if viewed along their main axis, statistically are not circular, but have a flattened interface. This effect brings the helices closer to each other and creates a tighter structural packing. The results provide an interesting insight into the aspects of protein structure and folding.