Secondary structure of a core protein from pig skin proteodermatan sulfate: Cd and fourier transform ir spectroscopic studies in solution
Secondary structure of a core protein from pig skin proteodermatan sulfate: Cd and fourier transform ir spectroscopic studies in solution
复制标题
猪皮硫酸原皮素核心蛋白的二级结构:溶液中的镉和傅里叶变换红外光谱研究
作者:
V. Renugopalakrishnan;S. Damle;P. Horowitz;S. Moore;T. B. Hutson;J. D. Gregory
The secondary structure of a 38 kDa core protein from pig skin proteodermatan sulfate (PDS), was investigated in solution using CD and Fourier transform (FT) ir spectroscopy. Both techniques generally have provided complementary data on the secondary structures of proteins. CD spectral analysis has shown that the core protein contains 60% β‐turn and α‐helical structures, the rest being “unordered” structure. FT ir data do not permit calculation of quantitative contributions of substructures, at the present time, to the overall secondary structure of the core protein. CD spectrum of the intact PDS is similar to the core protein CD spectrum.
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DOI:
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发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Rosenberg,LC;Choi,HU;Tang,LH;Johnson,TL;Pal,S;Webber,C;Reiner,A;Poole,AR
通讯作者:
Poole,AR
DOI:
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发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Iozzo,RV;Wight,TN
通讯作者:
Wight,TN
DOI:
--
发表时间:
1983
期刊:
Laboratory investigation; a journal of technical methods and pathology
影响因子:
--
作者:
Klintworth,GK;Smith,CF
通讯作者:
Smith,CF
DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Gregory,JD;Cöster,L;Damle,SP
通讯作者:
Damle,SP
影响因子:
11.2
作者:
Brennan,MJ;Oldberg,A;Hayman,EG;Ruoslahti,E
通讯作者:
Ruoslahti,E