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The role of local tight packing of hydrophobic groups in β‐structure
Author(s) -
Vtyurin Nickolie
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340150108
Subject(s) - materials science , chemical physics , chemistry
An analysis of the tendency of hydrophobic groups to tight packing on the surface of β‐sheets based on well‐known parameters of β‐sheets and hydrophobic groups was conducted. This analysis shows the existence of very limited numbers and clearly outlined architecture families of regular parts for the majority of β‐structure‐containing domains. Each family of architecture strongly depends on the number of β‐strands in the pure β‐domains and on the existence and number of additional α‐helixes and on the mutual arrangements β‐strands and α‐helixes along the chain in mixed α/β‐domains. This paper demonstrates that the tendency of hydrophobic groups to the local tight packing on the surface of β‐sheets is probably the main reason for the twist of β‐sheets. © 1993 Wiley‐Liss, Inc.