Stereospecific assignments of side‐chain protons and characterization of torsion angles in Eglin c

Stereospecific assignments were obtained in the protein Eglin c for β‐methylene protons of 9 out of the 24 residues with AMX symmetry, for three residues with long side chains and for the γ‐methyl groups of 8 out of the 11 valines. This was achieved by analyzing the cross‐peak multiplet structures i...

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Bibliographic Details
Published inEuropean journal of biochemistry Vol. 164; no. 3; pp. 625 - 635
Main Authors HYBERTS, Sven G., MÄRKI, Walter, WAGNER, Gerhard
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 04.05.1987
Blackwell
Subjects
Applied sciences
eglin c
Exact sciences and technology
Magnetic Resonance Spectroscopy
Mathematics
nuclear Overhauser effect
Other techniques and industries
Protein Conformation
Proteins
Protons
Serpins
Valine
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Summary:Stereospecific assignments were obtained in the protein Eglin c for β‐methylene protons of 9 out of the 24 residues with AMX symmetry, for three residues with long side chains and for the γ‐methyl groups of 8 out of the 11 valines. This was achieved by analyzing the cross‐peak multiplet structures in two‐dimensional correlated spectra with spectral simulations and peak fitting, and by quantitative measurements of intraresidue nuclear Overhauser enhancements. In addition to the stereospecific assignments, information on the torsion angels φ and X1 was obtained. To estimate inferences of internal motions on this analysis, the effect of uniform averaging within a certain range of the torsion angle X1 on cross‐peak multiplet structures and on relative intraresidue nuclear Overhauser enhancement is discussed.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1987.tb11173.x