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The role of local tight packing of hydrophobic groups in β‐structure

 

作者: Nickolie Vtyurin,  

 

期刊: Proteins: Structure, Function, and Bioinformatics  (WILEY Available online 1993)
卷期: Volume 15, issue 1  

页码: 62-70

 

ISSN:0887-3585

 

年代: 1993

 

DOI:10.1002/prot.340150108

 

出版商: Wiley Subscription Services, Inc., A Wiley Company

 

关键词: β‐sheet domain;globular proteins;three‐dimensional structure;twist

 

数据来源: WILEY

 

摘要:

AbstractAn 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 o

 

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