Variability in the pKa of histidine side-chains correlates with burial within proteins (Q44125134)

30 November 2017

title

Variability in the pKa of histidine side-chains correlates with burial within proteins (English)

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30 November 2017

Stephen P Edgcomb

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30 November 2017

Kenneth P Murphy

series ordinal

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30 November 2017

language of work or name

English

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publication date

1 October 2002

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30 November 2017

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30 November 2017

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30 November 2017

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30 November 2017

page(s)

1-6

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Determination of pKa values of the histidine side chains of phosphatidylinositol‐specific phospholipase C from Bacillus cereus by NMR spectroscopy and site‐directed mutagenesis

30 November 2017

cites work

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Protonation Behavior of Histidine 24 and Histidine 119 in Forming the pH 4 Folding Intermediate of Apomyoglobin

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Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange.

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His ... Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymes

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Electrostatic forces in two lysozymes: calculations and measurements of histidine pKa values

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

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High apparent dielectric constants in the interior of a protein reflect water penetration

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The determinants of pKas in proteins

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Electrostatic calculations of side-chain pK(a) values in myoglobin and comparison with NMR data for histidines

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Contributions of the ionizable amino acids to the stability of staphylococcal nuclease.

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Use of 1H NMR Spectroscopy and Computer Simulations To Analyze Histidine pKa Changes in a Protein Tyrosine Phosphatase: Experimental and Theoretical Determination of Electrostatic Properties in a Small Protein

21 January 2018

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The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules

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Structure of phosphate-free ribonuclease A refined at 1.26 .ANG

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The interpretation of protein structures: Estimation of static accessibility

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Residue depth: a novel parameter for the analysis of protein structure and stability.

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Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain

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Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin A.alpha

21 January 2018

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Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy

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Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignments

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21 January 2018

Identifiers

DOI

10.1002/PROT.10177

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30 November 2017

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