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Related Experiment Videos

Conformational mobility in cyclic oligopeptides

K D Kopple1, J W Bean, K K Bhandary

  • 1Department of Physical and Structural Chemistry, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406.

Biopolymers
|July 1, 1993
PubMed
Summary
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Two cyclic hexapeptides showed distinct backbone conformations and mobilities. Nuclear magnetic resonance studies revealed conformational heterogeneity in cyclic oligopeptides, impacting their structural definitions.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Physics

Background:

  • Cyclic oligopeptides are often assumed to possess well-defined backbone structures.
  • Understanding the conformational dynamics of these molecules is crucial for their biological function.

Purpose of the Study:

  • To analyze the backbone conformations of two isomeric cyclic hexapeptides.
  • To investigate potential differences in internal mobility between these isomers.
  • To review existing evidence on backbone conformational mobility in cyclic oligopeptides.

Main Methods:

  • Nuclear Overhauser effect (NOE) constrained distance geometry conformation search.
  • 13C relaxation studies.
  • Review of experimental evidence on cyclic oligopeptide mobility.

Related Experiment Videos

  • Nuclear magnetic resonance (NMR) line-shape studies at low temperatures (down to 200 K).

    • Main Results:

    • One cyclic hexapeptide isomer exhibited a narrowly defined backbone conformation.
    • The other isomer showed significant conformational ambiguity in parts of its structure.
    • Preliminary 13C relaxation data suggested differences in internal mobility correlating with conformational definition.
    • Conformational heterogeneity, including peptide bond rotation, is a common phenomenon in cyclic oligopeptides.
    • NMR line-shape analysis can detect backbone motions with activation barriers as low as 10 kcal/mole.

    Conclusions:

    • Isomeric cyclic hexapeptides can display distinct conformational behaviors and internal mobilities.
    • Conformational heterogeneity is prevalent in cyclic oligopeptides, challenging the notion of universally rigid backbones.
    • NMR spectroscopy, particularly at low temperatures, is a powerful tool for probing backbone dynamics, though limitations exist for very low energy barriers.