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1H And 13C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins

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1H And 13C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins (English)

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D. Neri

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Kurt Wüthrich

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3

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K. Wüthrich

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author name string

G. Otting

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2

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publication date

January 1990

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published in

Tetrahedron

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volume

46

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issue

9

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page(s)

3287-3296

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cites work

Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

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Two-dimensional NMR and protein structure.

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Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy

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Protein structures from NMR.

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What can two-dimensional NMR tell us about proteins?

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Protein structure determination in solution by nuclear magnetic resonance spectroscopy

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Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry

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The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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Stereospecificity of the reductoisomerase-catalyzed step in the pathway of biosynthesis of valine and leucine

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Letter: Enzymatic discrimination between diastereotopic enol faces in the dehydrase step of valine biosynthesis

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Stereochemistry of valine and isoleucine biosynthesis

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Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

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Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

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High field13C NMR studies at 90.5 MHz of the methyl groups in the basic pancreatic trypsin inhibitor

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High-field carbon-13 nuclear magnetic resonance studies at 90.5 MHz of the basic pancreatic trypsin inhibitor

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Homology among DNA-binding proteins suggests use of a conserved super-secondary structure

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10.1016/S0040-4020(01)85464-8

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(Q57912201)

1H And 13C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins

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