Method of determining protein conformations by the two-dimensional nuclear overhauser enhancement spectroscopy data

Simon Sherman, A. M. Andrianov, A. A. Akhrem

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

A method is suggested to determine the most probable values of the angles, y of the protein backbone by the data on the availability and absence of d connectivities in the two-dimensional nuclear Overhauser enhancement spectra. In view of this, the dependences of the protonproton distances in dipeptide units of L-amino acid residues on the dihedral angles tp, y, x, are considered and the conformational states of amino acid residues of the proteins with the known spatial structure are analysed statistically. The potentialities of the method are assessed with the aid of model spectral nuclear magnetic resonance (NMR) parameters obtained from the X-ray data for the bovine pancreatic trypsin inhibitor and avian pancreatic polypeptide. It is shown that the developed procedure of structural interpretation of the NMR data allows one to correctly reproduce the local conformation of the protein backbone. The obtained backbone conformation may serve as a starting point to build and refine molecular threedimensional structure.

Original languageEnglish (US)
Pages (from-to)869-884
Number of pages16
JournalJournal of Biomolecular Structure and Dynamics
Volume4
Issue number5
DOIs
StatePublished - Jan 1 1987

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Protein Conformation
Spectrum Analysis
Magnetic Resonance Spectroscopy
Amino Acids
Aprotinin
Dipeptides
Molecular Structure
Proteins
X-Rays

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Method of determining protein conformations by the two-dimensional nuclear overhauser enhancement spectroscopy data. / Sherman, Simon; Andrianov, A. M.; Akhrem, A. A.

In: Journal of Biomolecular Structure and Dynamics, Vol. 4, No. 5, 01.01.1987, p. 869-884.

Research output: Contribution to journalArticle

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