PMID: 8942977Nov 26, 1996Paper

A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy

Proceedings of the National Academy of Sciences of the United States of America
K FurukawaH Nakamura

Abstract

A small globular protein, the third repeat of the c-Myb DNA-binding domain, which is composed of 54 amino acid residues, was engineered so as to understand the structural uniqueness of native proteins. This small protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181) substituted with Leu residues, showed multiple conformations, as monitored by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled proteins. The increase in the side-chain conformational entropy, caused by changing the Ile to a Leu residue on an alpha-helix, could engender the lack of structural uniqueness. In native proteins, the conformations of not only the beta-branched side chains, but also those of the neighboring bulky side chains, can be greatly restricted, depending upon the local backbone structure.

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Citations

Jul 31, 2013·Archives of Biochemistry and Biophysics·Satomi InabaMasayuki Oda
Apr 7, 2000·Protein Science : a Publication of the Protein Society·O V GalzitskayaH Nakamura
Sep 15, 2007·Proceedings of the National Academy of Sciences of the United States of America·Jaime López de la OsaDouglas V Laurents
Nov 5, 2003·Proceedings of the National Academy of Sciences of the United States of America·Stefano GianniAlan R Fersht
Nov 18, 2005·Journal of Molecular Biology·Yasuhiro IsogaiMotonori Ota

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