COMPUTED CIRCULAR DICHROISM SPECTRA FOR EVALUATION OF PROTEIN CONFORMATION
COMPUTED CIRCULAR DICHROISM SPECTRA FOR EVALUATION OF PROTEIN CONFORMATION
复制标题
DOI:
10.1021/bi00838a031
复制
发表时间:
1969-01-01
期刊:
影响因子:
2.9
通讯作者:
FASMAN, GD
中科院分区:
文献类型:
--
作者:
GREENFIE.N;FASMAN, GD
Circular dichroism curves of poly-L-lysine con-taining varying amounts of a helix,/3-pleatedsheet, and random coil segments have been computed in the 190-250-µ region. The application of these curves for determining protein conformation is discussed. The circular dichroism curves of several proteins, whose three-dimensional structures are known from X-ray diffraction studies, have been fitted by a linear combination of the threereference structures in the 208-240-µ region. Theresults show that these computed