C
Chih Chin Huang
Researcher at Duke University
Publications - 4
Citations - 1163
Chih Chin Huang is an academic researcher from Duke University. The author has contributed to research in topics: Binding site & Histidine. The author has an hindex of 4, co-authored 4 publications receiving 1040 citations.
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Journal ArticleDOI
Function and mechanism of zinc metalloenzymes.
TL;DR: These studies demonstrate that the chemical nature of the direct ligands and the structure of the surrounding hydrogen bond network are crucial for both the activity of carbonic anhydrase and the metal ion affinity of the zinc-binding site.
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High-level 2H/13C/15N labeling of proteins for NMR studies
Ronald A. Venters,Chih Chin Huang,Bennett T. Farmer,Ronald Trolard,Leonard D. Spicer,Carol A. Fierke +5 more
TL;DR: The protein human carbonic anhydrase II has been isotopically labeled with 2H, 13C and 15N for high-resolution NMR assignment studies and pulse sequence development to increase the sensitivity of several key 1H/13C/15N triple-resonance correlation experiments.
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Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity.
TL;DR: Structural and functional analysis of variants in which the zinc ligands H94 and H119 are substituted with asparagine and glutamine, and comparison with results obtained with aspartate and glutamate substitutions indicate that the neutral ligand field provided by the protein optimizes the electrostatic environment for the catalytic function of the metal ion, including stabilization of bound anions.
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Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state.
TL;DR: Data suggest that FTase catalyzes protein farnesylation by an associative mechanism with an "exploded" transition state where the metal-bound peptide/protein sulfur has a partial negative charge, the C1 of FPP has apartial positive charge, and the bridge oxygen between C1 and the alpha phosphate of F PP has a Partial negative charge.