Secondary structure of a core protein from pig skin proteodermatan sulfate: Cd and fourier transform ir spectroscopic studies in solution

V. Renugopalakrishnan, Shridhar P. Damle, Paul M. Horowitz, Sheri Moore, Timothy B. Hutson, John D. Gregory

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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% 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.

Original languageEnglish (US)
Pages (from-to)1923-1933
Number of pages11
JournalBiopolymers
Volume28
Issue number11
DOIs
StatePublished - Nov 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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