Factors Governing the Protonation State of Zn-Bound Histidine in Proteins: A DFT/CDM Study-Reference-Cited by-同舟云学术

Factors Governing the Protonation State of Zn-Bound Histidine in Proteins: A DFT/CDM Study

Published:2004-02-06 Issue:8 Volume:126 Page:2602-2612
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lin ¹,Lim Carmay¹

Affiliation:

1. Contribution from the Institute of Biomedical Science, Academic Sinica, Taipei 11529, Taiwan R.O.C., and Department of Chemistry, National Tsing Hua University, Hsinchu 300, Taiwan R.O.C.

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja038827r

Reference78 articles.

1. Structural Biology of Zinc

2. ZINC PROTEINS: Enzymes, Storage Proteins, Transcription Factors, and Replication Proteins

3. Analysis of zinc binding sites in protein crystal structures

4. Carboxylate-histidine-zinc interactions in protein structure and function

5. Structural Influence of Hydrophobic Core Residues on Metal Binding and Specificity in Carbonic Anhydrase II,

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