Journal article

A peptide corresponding to residues Asp177 to Asn208 of human cyclin A forms an alpha-helix

JS Fan, HC Cheng, MJ Zhang

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 1998

Abstract

Cyclins are essential activators of eukaryotic cell cycle-regulating enzymes called cyclin-dependent kinases (CDKs). The binding of cyclins to CDKs is mediated by a structural motif comprising a five-helix bundle called the cyclin fold and an additional helix (the N-terminal alpha-helix) located N-terminal to the cyclin fold. In this work, we examine, using CD and NMR spectroscopy, the structure of a 32-residue synthetic peptide derived from the segment (Asp177 to Asn208) corresponding to the N-terminal alpha-helix of human cyclin A. CD spectroscopic analysis of the peptide revealed that trifluoroethanol (TFE) can induce the peptide to assume a stable alpha-helix conformation. Two-dimensiona..

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