BETA-II CONFORMATION OF ALL-BETA PROTEINS CAN BE DISTINGUISHED FROM UNORDERED FORM BY CIRCULAR-DICHROISM

被引:87
作者
WU, J [1 ]
YANG, JT [1 ]
WU, CSC [1 ]
机构
[1] UNIV CALIF SAN FRANCISCO,CARDIOVASC RES INST,SAN FRANCISCO,CA 94143
关键词
D O I
10.1016/0003-2697(92)90479-Q
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The CD spectrum of certain all-β globular proteins resembles that of unfolded proteins with a characteristic negative band around 200 nm. The conformation of this class is tentatively termed β-II, which had two features that were absent for unfolded proteins. First, β-II proteins usually had CD bands due to aromatic side groups in the near-ultraviolet region. Second, the CD intensities both in the far- and in the near-uv region of these compact and rigid proteins usually showed a sharp transition upon thermal denaturation, whereas those of an unordered form changed linearly with rising temperature. © 1992.
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页码:359 / 364
页数:6
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