A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.
about
Merging molecular mechanism and evolution: theory and computation at the interface of biophysics and evolutionary population geneticsExperimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymesContribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozymeEffect of foreign N-terminal residues on the conformational stability of human lysozymeEntropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetrySubunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acidRole of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozymeRole of amino acid residues in left-handed helical conformation for the conformational stability of a proteinPositive contribution of hydration structure on the surface of human lysozyme to the conformational stabilityEngineering hyperthermostability into a GH11 xylanase is mediated by subtle changes to protein structureStructural and thermodynamic responses of mutations at a Ca2+ binding site engineered into human lysozymeHyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostabilityThe molecular basis of the effect of temperature on enzyme activitySolvent accessibility, protein surfaces, and protein foldingThe nuclear matrix is a thermolabile cellular structureCalculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot springA model of proteostatic energy cost and its use in analysis of proteome trends and sequence evolutionThermal, chemical and pH induced unfolding of turmeric root lectin: modes of denaturationStreptococcus pneumoniae TIGR4 Flavodoxin: Structural and Biophysical Characterization of a Novel Drug TargetStructural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase IIRobustness of atomistic Gō models in predicting native-like folding intermediates.Reversible unfolding and refolding behavior of a monomeric aldolase from Staphylococcus aureusA new approach for determining the stability of recombinant human epidermal growth factor by thermal Fourier transform infrared (FTIR) microspectroscopy.Effect of sequential deletion of extra N-terminal residues on the structure and stability of yeast iso-1-cytochrome-c.Inactivation and unfolding of protein tyrosine phosphatase from Thermus thermophilus HB27 during urea and guanidine hydrochloride denaturation.Fractal properties of lysozyme: a neutron scattering study.Effects of temperature on food proteins and its implications on functional properties.Dynamics-stability relationships in apo- and holomyoglobin: a combined neutron scattering and molecular dynamics simulations studyDifferential modulation in binding of ketoprofen to bovine serum albumin in the presence and absence of surfactants: spectroscopic and calorimetric insights.Thermodynamic properties of purple membrane.Protein biophysics explains why highly abundant proteins evolve slowlyA linkage analysis toolkit for studying allosteric networks in ion channels.Redesigned HIV antibodies exhibit enhanced neutralizing potency and breadth.Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c.Interaction of a designed interleukin-10 epitope mimic with an antibody studied by isothermal titration microcalorimetry.Stabilizing the subtilisin BPN' pro-domain by phage display selection: how restrictive is the amino acid code for maximum protein stability?Revisiting the myths of protein interior: studying proteins with mass-fractal hydrophobicity-fractal and polarizability-fractal dimensionsCrosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization.The nucleotide exchange factor Ric-8A is a chaperone for the conformationally dynamic nucleotide-free state of Gαi1.Evidence, from simulations, of a single state with residual native structure at the thermal denaturation midpoint of a small globular protein
P2860
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P2860
A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study.
description
1974 nî lūn-bûn
@nan
1974 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1974 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1974年の論文
@ja
1974年論文
@yue
1974年論文
@zh-hant
1974年論文
@zh-hk
1974年論文
@zh-mo
1974年論文
@zh-tw
1974年论文
@wuu
name
A thermodynamic approach to th ...... ructure: a calorimetric study.
@ast
A thermodynamic approach to th ...... ructure: a calorimetric study.
@en
type
label
A thermodynamic approach to th ...... ructure: a calorimetric study.
@ast
A thermodynamic approach to th ...... ructure: a calorimetric study.
@en
prefLabel
A thermodynamic approach to th ...... ructure: a calorimetric study.
@ast
A thermodynamic approach to th ...... ructure: a calorimetric study.
@en
P1476
A thermodynamic approach to th ...... ructure: a calorimetric study.
@en
P2093
Khechinashvili NN
Privalov PL
P304
P356
10.1016/0022-2836(74)90188-0
P407
P577
1974-07-01T00:00:00Z