Conformational studies of cyclic peptide structures in solution from 1H-Nmr data by distance geometry calculation and restrained energy minimization

H. Senn, H. R. Loosli, M. Sanner, Werner Braun

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The three-dimensional structure of a cyclic bouvardin analogue, cyclo (-Pro-MeTyr-Ala-MeTyr-MeTyr-D-Ala-) has been determined by distance geometry calculation and restrained energy minimization from nmr data. The preparation of the input for the distance geometry calculations, the modification of the amino acid library, and the analysis of the structures were done with the aid of a recently developed software package, GEOM. A great variety of different initial structures were explored to check the uniqueness of the determined solution structure. Calculations with 500 different initial structures and two different strategies led to a uniquely determined backbone conformation with a root mean square deviations value of 0.4 Å. The backbone structure consists of two β-turns, a β-II turn at Pro1-MeTyr2, and a β-VI turn at MeTyr4-MeTyr5. The efficiency of the two calculation strategies were compared in order to propose an optimal means for performing distance geometry calculations with cyclic structures.

Original languageEnglish (US)
Pages (from-to)1387-1400
Number of pages14
JournalBiopolymers
Volume29
Issue number10-11
DOIs
StatePublished - 1990
Externally publishedYes

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bouvardin
Cyclic Peptides
Software
Amino Acids
Geometry
Software packages
Conformations
Amino acids

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

Conformational studies of cyclic peptide structures in solution from 1H-Nmr data by distance geometry calculation and restrained energy minimization. / Senn, H.; Loosli, H. R.; Sanner, M.; Braun, Werner.

In: Biopolymers, Vol. 29, No. 10-11, 1990, p. 1387-1400.

Research output: Contribution to journalArticle

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