Literature DB >> 10698273

NMR measurements of proton exchange between solvent and peptides and proteins.

J Wójcik1, K Ruszczyńska, I Zhukov, A Ejchart.   

Abstract

Scope and limitations of the NMR based methods, equilibration and magnetization transfer, for measuring proton exchange rates of amide protons in peptides and proteins with water protons are discussed. Equilibration is applied to very slow processes detected by hydrogen-deuterium exchange after a solute is dissolved in D2O. Magnetization transfer allows to study moderately rapid processes in H2O. A number of precautions should be undertaken in order to avoid systemic errors inherent in the magnetization transfer method.

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Year:  1999        PMID: 10698273

Source DB:  PubMed          Journal:  Acta Biochim Pol        ISSN: 0001-527X            Impact factor:   2.149


  3 in total

1.  Rapid and accurate processing method for amide proton exchange rate measurement in proteins.

Authors:  Harri Koskela; Outi Heikkinen; Ilkka Kilpeläinen; Sami Heikkinen
Journal:  J Biomol NMR       Date:  2007-02-14       Impact factor: 2.835

2.  Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.

Authors:  Juan-Miguel Lopez del Amo; Uwe Fink; Bernd Reif
Journal:  J Biomol NMR       Date:  2010-10-20       Impact factor: 2.835

3.  Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly.

Authors:  Tomasz Kochańczyk; Michał Nowakowski; Dominika Wojewska; Anna Kocyła; Andrzej Ejchart; Wiktor Koźmiński; Artur Krężel
Journal:  Sci Rep       Date:  2016-11-03       Impact factor: 4.379

  3 in total

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