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    • ProtonNMR studies of peptide conformations

      P Balaram

      Volume 95 Issue 1-2 July 1985 pp 21-38

    • Fulltext

       

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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/095/01-02/0021-0038

    • Keywords

       

      Nuclear magnetic resonance; peptide conformation; hydrogen bonding; peptide aggregation; nuclear-Overhauser effects

    • Abstract

       

      This article reviews recent1HNMR studies on peptides carried out in the author’s laboratory. Methods for the delineation of hydrogen bonded NH groups are discussed and exemplified by studies of conformationally constrained peptides. The application of concentration dependences ofNMR parameters for NH groups in peptides to the study of peptide aggregation in apolar solvents is considered. Investigations on chemotactic peptide analogs and suzukacillin fragments are briefly summarized. Nuclear-Overhauser effect studies on β-sheet and β-turn conformational models are described.NMR studies on conformational transitions accompanying dissolution of single crystals are illustrated by a study of a peptide containing a -Pro-Pro- segment.

    • Author Affiliations

       

      P Balaram1

      1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore - 560012, India

    • Dates

       
      Published
      July 1985

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