Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H−15N NMR Spectroscopy-Reference-Cited by-同舟云学术

Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H−15N NMR Spectroscopy

Published:2010-12-27 Issue:4 Volume:133 Page:909-919
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Esadze Alexandre¹,Li Da-Wei²,Wang Tianzhi¹,Brüschweiler Rafael²,Iwahara Junji¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555, United States

2. Chemical Sciences Laboratory, Department of Chemistry and Biochemistry, and National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32306, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja107847d

Reference86 articles.

1. Proton exchange rates from amino acid side chains— implications for image contrast

2. Exchange Rate Constants of Invisible Protons in Proteins Determined by NMR Spectroscopy

3. Heteronuclear NMR Spectroscopy for Lysine NH3 Groups in Proteins: Unique Effect of Water Exchange on 15N Transverse Relaxation

4. Unambiguous Determination of the Ionization State of a Glycoside Hydrolase Active Site Lysine by 1H−15N Heteronuclear Correlation Spectroscopy

5. Direct Evidence for Deprotonation of a Lysine Side Chain Buried in the Hydrophobic Core of a Protein

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