Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy.
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Ionizable Nitroxides for Studying Local Electrostatic Properties of Lipid Bilayers and Protein Systems by EPRDomain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?Protein dielectric constants determined from NMR chemical shift perturbationsMapping local protein electrostatics by EPR of pH-sensitive thiol-specific nitroxide.Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stabilitySite-specific contributions to the pH dependence of protein stabilityAn accurate density functional theory based estimation of pK(a) values of polar residues combined with experimental data: from amino acids to minimal proteins.pH dependence of amide chemical shifts in natively disordered polypeptides detects medium-range interactions with ionizable residues.Segmental polymorphism in a functional amyloid.Electrostatic Energetics of Bacillus subtilis Ribonuclease P Protein Determined by Nuclear Magnetic Resonance-Based Histidine pKa Measurements.Thermodynamics of protein denatured states.pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability(1)H, (13)C, and (15)N resonance assignment of photoactive yellow protein.pK(a) values for the unfolded state under native conditions explain the pH-dependent stability of PGB1.Electrostatic effects in unfolded staphylococcal nuclease.100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G.Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.Putative one-pot prebiotic polypeptides with ribonucleolytic activity.Characterization of the APLF FHA-XRCC1 phosphopeptide interaction and its structural and functional implications.A 13C-detected 15N double-quantum NMR experiment to probe arginine side-chain guanidinium 15Nη chemical shifts.Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random-coil-like pKa values.Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.
P2860
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P2860
Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@ast
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@en
type
label
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@ast
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@en
prefLabel
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@ast
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@en
P356
P1476
Measurement of side-chain carb ...... multinuclear NMR spectroscopy.
@en
P2093
Martin Tollinger
P304
P356
10.1021/JA020066P
P407
P577
2002-05-01T00:00:00Z