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The peptide chain of tyrosyl tRNA synthetase: No evidence for a super-secondary structure of four α-helices

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
76
Issue
3
Identifiers
DOI: 10.1016/0006-291x(77)91560-1
Disciplines
  • Biology

Abstract

Abstract A detailed backbone model has been built for 274 residues of tyrosyl tRNA synthetase, based on an X-ray diffraction study. This includes eight helical sections and a six-stranded pleated sheet. The four helices near the carboxyl terminal end are not arranged like the helices of TMV disk protein and hemerythrin, and the structure gives no support to the idea that four antiparallel helices form a common structural unit in proteins.

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