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Resonance assignment of methionine methyl groups and chi 3 angular information from long-range proton-carbon and carbon-carbon J correlation in a calmodulin-peptide complex

Bax, A ; Delaglio, F ; Grzesiek, S ; Vuister, G W

Journal of biomolecular NMR, 1994-11, Vol.4 (6), p.787-797 [Periódico revisado por pares]

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Título:
Resonance assignment of methionine methyl groups and chi 3 angular information from long-range proton-carbon and carbon-carbon J correlation in a calmodulin-peptide complex
Autor: Bax, A ; Delaglio, F ; Grzesiek, S ; Vuister, G W
Assuntos: Amino Acid Sequence ; Calmodulin - chemistry ; Calmodulin-Binding Proteins - chemistry ; Carbon ; Magnetic Resonance Spectroscopy ; Methionine - chemistry ; Molecular Sequence Data ; Myosin-Light-Chain Kinase - chemistry ; Peptides - chemistry ; Protons
É parte de: Journal of biomolecular NMR, 1994-11, Vol.4 (6), p.787-797
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Several simple 3D experiments are used to provide J correlations between methionine C epsilon methyl carbons and either the C gamma H2 protons or C beta and C gamma. The intensity of the J correlations provides information on the size of the three-bond J couplings and thereby on the chi 3 torsion angle. In addition, a simple 3D version of the HMBC experiment provides a sensitive link between the C epsilon H3 methyl protons and C gamma. The methods are demonstrated for a 20 kDa complex between calmodulin and a 26-residue peptide fragment of skeletal muscle myosin light chain kinase.
Editor: Netherlands
Idioma: Inglês

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