Conformational Studies of Boc-L-Pro-L-Pra-Gly-OMe by X-Ray,

Abstract

L-Propargylglycine (L-Pra) has been revealed to be a natural occuring antimetabolite of methionine and leucine. Its synthetic racemate is also a powerful inhibitor of microbial growth. In search of certain enzyme inactivators. L-Pra was incorporated into dipeptides that resulted in strong suicidal substrates for microorganisms. Sinc procollagen consists mainly of the Pro-X-Gly unit which is post-translationally hydroxylated by the enzyme prolyl-4-hydroxylase (when X=Pro), we replaced X by L-Pra and studied the interaction of the resulting tripeptide with the enzyme. The synthesized peptide was characterized by NMR and mass spectrometry and its crystal structure was established by X-ray diffraction analysis.

Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1992
Accession Number
ADP008368

Entities

People

  • B. Hemmasi
  • E. Bayer
  • H. Willisch
  • W. Hiller

Organizations

  • University of Tübingen

Tags

DTIC Thesaurus Topics

  • Chemistry
  • Crystal Structure
  • Diffraction
  • Diffraction Analysis
  • Mass Spectrometry
  • Spectrometry
  • X Rays
  • X-Ray Diffraction

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry

Technology Areas

  • Biotechnology