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Nuclear magnetic resonance studies and molecular dynamics simulations of the solution conformation of a ‘designed’, α-helical peptide


Klaus, Werner; Moser, Rudolf (1992). Nuclear magnetic resonance studies and molecular dynamics simulations of the solution conformation of a ‘designed’, α-helical peptide. Protein Engineering, Design & Selection, 5(4):333-341.

Abstract

The complete three-dimensional structure in methanol of an amphipathic a-helical peptide, that has been designed by taking into account the three-dimensional structures of small haemolytic peptides, secondary structure prediction algorithms and the well documented literature on α-helix stabilizing factors, has been elucidated by two-dimensional NMR spectroscopy. Initially various two-dimensional spectra (COSY, TOCSY, and NOESY) allowed the complete sequence specific assignment of all signals in the 1H spectrum. Consequently trial structures were generated which were then subjected to molecular dynamics simulations using 121 NOE-derived distances and 25 vicinal coupling constant values as structural restraints to give a final set of calculated structures. These structures are in complete agreement with the results of a circular dichroism study and reveal that the peptide adopted a highly ordered a-helical conformation. Details of the structure which throw light on future peptide/protein design are discussed

Abstract

The complete three-dimensional structure in methanol of an amphipathic a-helical peptide, that has been designed by taking into account the three-dimensional structures of small haemolytic peptides, secondary structure prediction algorithms and the well documented literature on α-helix stabilizing factors, has been elucidated by two-dimensional NMR spectroscopy. Initially various two-dimensional spectra (COSY, TOCSY, and NOESY) allowed the complete sequence specific assignment of all signals in the 1H spectrum. Consequently trial structures were generated which were then subjected to molecular dynamics simulations using 121 NOE-derived distances and 25 vicinal coupling constant values as structural restraints to give a final set of calculated structures. These structures are in complete agreement with the results of a circular dichroism study and reveal that the peptide adopted a highly ordered a-helical conformation. Details of the structure which throw light on future peptide/protein design are discussed

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Scopus Subject Areas:Life Sciences > Biotechnology
Physical Sciences > Bioengineering
Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Language:English
Date:1 January 1992
Deposited On:16 Oct 2018 14:37
Last Modified:31 Jul 2020 02:22
Publisher:Oxford University Press
ISSN:1741-0126
OA Status:Green
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/protein/5.4.333
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicenceoxford101093protein54333 (Library Catalogue)

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