TY - JOUR
T1 - Secondary structure of a core protein from pig skin proteodermatan sulfate
T2 - Cd and fourier transform ir spectroscopic studies in solution
AU - Renugopalakrishnan, V.
AU - Damle, Shridhar P.
AU - Horowitz, Paul M.
AU - Moore, Sheri
AU - Hutson, Timothy B.
AU - Gregory, John D.
PY - 1989/11
Y1 - 1989/11
N2 - 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.
AB - 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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U2 - 10.1002/bip.360281109
DO - 10.1002/bip.360281109
M3 - Article
C2 - 2597740
AN - SCOPUS:0024358839
VL - 28
SP - 1923
EP - 1933
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 11
ER -