The role of dense local packing of hydrophobic groups in β-structural proteins

Authors

  • N. N. Vtyurin Institute of Molecular Genetics, Academy of Sciences of the USSR Moscow, USSR Author

DOI:

https://doi.org/10.7124/bc.000266

Abstract

The study demonstrates that the tendency of hydrophobic groups to the dense local packing on the surface of β-structural sheets is probably the main reason for the twist of β-structural sheets. To the author's opinion, this fact makes it possible to interpret in a new fashion the architecture of almost all β-structure-containing domains. The majority of β-structure-containing domains are shown to fall into several clearly-outlined groups with the architectural properties depending on the number and mutual disposition along the chain of the elements of secondary structure (β-strands and α-helixes) forming the domain.

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Published

1990-05-20

Issue

Section

Structure and Function of Biopolymers