Direct Evidence for Deprotonation of a Lysine Side Chain Buried in the Hydrophobic Core of a Protein-Reference-Cited by-同舟云学术

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

Published:2008-05-01 Issue:21 Volume:130 Page:6714-6715
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Takayama Yuki¹,Castañeda Carlos A.¹,Chimenti Michael¹,García-Moreno Bertrand¹,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 77555-0647, and Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja801731g

Reference17 articles.

1. Experimental measurement of the effective dielectric in the hydrophobic core of a protein

2. In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core

3. Experimental pKa Values of Buried Residues: Analysis with Continuum Methods and Role of Water Penetration

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

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