Abstract:
: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% beta-turn and alpha-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.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Renugopalakrishnan V,Damle SP,Horowitz PM,Moore S,Hutson TB,Gregory JDdoi
10.1002/bip.360281109subject
Has Abstractpub_date
1989-11-01 00:00:00pages
1923-33issue
11eissn
0006-3525issn
1097-0282journal_volume
28pub_type
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