Secondary structure of a core protein from pig skin proteodermatan sulfate: CD and Fourier transform IR spectroscopic studies in solution.

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

Biopolymers

journal_title

Biopolymers

authors

Renugopalakrishnan V,Damle SP,Horowitz PM,Moore S,Hutson TB,Gregory JD

doi

10.1002/bip.360281109

subject

Has Abstract

pub_date

1989-11-01 00:00:00

pages

1923-33

issue

11

eissn

0006-3525

issn

1097-0282

journal_volume

28

pub_type

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