Empirical relationships between protein structure and carboxyl pKa values in proteins.
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Positioning of proteins in membranes: a computational approachPPD v1.0--an integrated, web-accessible database of experimentally determined protein pKa valuesDNA lesion recognition by the bacterial repair enzyme MutMp K a Coupling at the Intein Active Site: Implications for the Coordination Mechanism of Protein Splicing with a Conserved AspartateBiochemical and Structural Studies of Conserved Maf Proteins Revealed Nucleotide Pyrophosphatases with a Preference for Modified NucleotidesProton binding to proteins: a free-energy component analysis using a dielectric continuum model.Exploration of glycosyl hydrolase family 75, a chitosanase from Aspergillus fumigatus.Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Effects of localized interactions and surface properties on stability of protein-based therapeutics.Remeasuring HEWL pK(a) values by NMR spectroscopy: methods, analysis, accuracy, and implications for theoretical pK(a) calculations.Uncovering the determinants of a highly perturbed tyrosine pKa in the active site of ketosteroid isomerase.Benchmarking pK(a) prediction.Stabilization of internal charges in a protein: water penetration or conformational change?NMR Determination of Protein pK(a) Values in the Solid StateLocal conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins.Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.pH dependence of amide chemical shifts in natively disordered polypeptides detects medium-range interactions with ionizable residues.Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changesEvidence for an elevated aspartate pK(a) in the active site of human aromataseRapid calculation of protein pKa values using Rosetta.Carboxyl pK(a) values, ion pairs, hydrogen bonding, and the pH-dependence of folding the hyperthermophile proteins Sac7d and Sso7dAn extracellular Cu2+ binding site in the voltage sensor of BK and Shaker potassium channelsA fast and accurate computational approach to protein ionization.Structures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions.Polysaccharide Nanoparticles for Efficient siRNA Targeting in Cancer Cells by Supramolecular pKa Shift.Determination of the gas-phase acidities of oligopeptides.Computational simulation strategies for analysis of multisubunit RNA polymerases.Reproducing basic pKa values for turkey ovomucoid third domain using a polarizable force field.Use of secondary structure element information in drug design: polypharmacology and conserved motifs in protein-ligand binding and protein-protein interfaces.The pKa Cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins.Using polarizable POSSIM force field and fuzzy-border continuum solvent model to calculate pK(a) shifts of protein residues.Calcium-dependent plasma membrane binding and cell lysis by perforin are mediated through its C2 domain: A critical role for aspartate residues 429, 435, 483, and 485 but not 491.Elucidation of isoform-dependent pH sensitivity of troponin i by NMR spectroscopy.Crystallization and preliminary X-ray analysis of human MTH1 with a homogeneous N-terminus.A summary of the measured pK values of the ionizable groups in folded proteins.pKa predictions for proteins, RNAs, and DNAs with the Gaussian dielectric function using DelPhi pKa.Dark states in monomeric red fluorescent proteins studied by fluorescence correlation and single molecule spectroscopy.Thermodynamic principles for the engineering of pH-driven conformational switches and acid insensitive proteins.MCCE2: improving protein pKa calculations with extensive side chain rotamer sampling.
P2860
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P2860
Empirical relationships between protein structure and carboxyl pKa values in proteins.
description
2002 nî lūn-bûn
@nan
2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@ast
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@en
type
label
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@ast
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@en
prefLabel
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@ast
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@en
P2093
P2860
P356
P1433
P1476
Empirical relationships between protein structure and carboxyl pKa values in proteins.
@en
P2093
Andrew D Robertson
Jan M Antosiewicz
William R Forsyth
P2860
P304
P356
10.1002/PROT.10174
P407
P577
2002-08-01T00:00:00Z