Modified Triple Resonance NMR Experiments with Optimized Sensitivity for Rapidly Exchanging Protons

Wolfgang Jahnke; Horst Kessler

doi:10.1002/anie.199504691

Modified Triple Resonance NMR Experiments with Optimized Sensitivity for Rapidly Exchanging Protons

Wolfgang Jahnke, Horst Kessler

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Technical University of Munich

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5 Scopus citations

Abstract

Fast exchange with surrounding water protons need not attenuate ¹H NMR signals of proteins in solution. A modified pulse sequence has been developed to increase the signal intensity of the amide protons; on the right the improvement in sensitivity (a → c) is shown for a selected residue in a protein. This new technique should aid elucidation of protein structures in solution. (Figure Presented.)

Original language	English
Pages (from-to)	469-471
Number of pages	3
Journal	Angewandte Chemie International Edition in English
Volume	34
Issue number	4
DOIs	https://doi.org/10.1002/anie.199504691
State	Published - 7 Mar 1995

Keywords

NMR spectroscopy
proteins
structure elucidation

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10.1002/anie.199504691

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title = "Modified Triple Resonance NMR Experiments with Optimized Sensitivity for Rapidly Exchanging Protons",

abstract = "Fast exchange with surrounding water protons need not attenuate 1H NMR signals of proteins in solution. A modified pulse sequence has been developed to increase the signal intensity of the amide protons; on the right the improvement in sensitivity (a → c) is shown for a selected residue in a protein. This new technique should aid elucidation of protein structures in solution. (Figure Presented.)",

keywords = "NMR spectroscopy, proteins, structure elucidation",

author = "Wolfgang Jahnke and Horst Kessler",

year = "1995",

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T1 - Modified Triple Resonance NMR Experiments with Optimized Sensitivity for Rapidly Exchanging Protons

AU - Jahnke, Wolfgang

AU - Kessler, Horst

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N2 - Fast exchange with surrounding water protons need not attenuate 1H NMR signals of proteins in solution. A modified pulse sequence has been developed to increase the signal intensity of the amide protons; on the right the improvement in sensitivity (a → c) is shown for a selected residue in a protein. This new technique should aid elucidation of protein structures in solution. (Figure Presented.)

AB - Fast exchange with surrounding water protons need not attenuate 1H NMR signals of proteins in solution. A modified pulse sequence has been developed to increase the signal intensity of the amide protons; on the right the improvement in sensitivity (a → c) is shown for a selected residue in a protein. This new technique should aid elucidation of protein structures in solution. (Figure Presented.)

KW - NMR spectroscopy

KW - proteins

KW - structure elucidation

UR - http://www.scopus.com/inward/record.url?scp=33751150517&partnerID=8YFLogxK

U2 - 10.1002/anie.199504691

DO - 10.1002/anie.199504691

M3 - Article

AN - SCOPUS:33751150517

SN - 0570-0833

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JO - Angewandte Chemie International Edition in English

JF - Angewandte Chemie International Edition in English

IS - 4

ER -

Modified Triple Resonance NMR Experiments with Optimized Sensitivity for Rapidly Exchanging Protons

Abstract

Keywords

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