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Structural characteristics and stabilizing principles of bent β‐strands in protein tertiary architectures
Author(s) -
Daffner Carola,
Chelvanayagam Gareth,
Argos Patrick
Publication year - 1994
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 - 10.1002/pro.5560030602
Subject(s) - bent molecular geometry , antiparallel (mathematics) , bending , crystallography , distortion (music) , protein tertiary structure , polar , materials science , chemistry , physics , composite material , amplifier , biochemistry , optoelectronics , cmos , quantum mechanics , astronomy , magnetic field
β‐Strands as constituents of β‐pleated sheets in protein tertiary structures often display considerable distortion from a purely extended conformation. The dislocation types are often characterized as “bulging,” “twisting,” and “bending.” The former 2 properties have been extensively studied and classified. In this work an investigation of bent β‐structures is undertaken. The structural characteristics examined included the bending angles within and out of the principal strand plane, their distribution among various strand types such as parallel and antiparallel, the amino acid preferences at bend sites, and the usage of charged and polar residues for stabilization through interactive anchoring with other atoms of the β‐sheet within which the bent strand lies.