about
The (1)H, (13)C, (15)N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopyUrea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsSignificant stabilization of ribonuclease A by additive effectsContribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease APressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal siteNonlinear least-squares data fitting in Excel spreadsheets.Human 60-kDa lysophospholipase contains an N-terminal L-asparaginase domain that is allosterically regulated by L-asparagine.pH dependence thermal stability of a chymotrypsin inhibitor from Schizolobium parahyba seeds.Cold instability of aponeocarzinostatin and its stabilization by labile chromophore.Oligomerization, conformational stability and thermal unfolding of Harpin, HrpZPss and its hypersensitive response-inducing c-terminal fragment, C-214-HrpZPss.Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.Heat capacity changes upon burial of polar and nonpolar groups in proteins.Trimethylamine-N-oxide switches from stabilizing nature: A mechanistic outlook through experimental techniques and molecular dynamics simulation.Replacing a single atom accelerates the folding of a protein and increases its thermostability.Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state.Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA.Refinement of noncalorimetric determination of the change in heat capacity, DeltaC(p), of protein unfolding and validation across a wide temperature range.Biphasic reductive unfolding of ribonuclease A is temperature dependent.Determining the conformational stability of a protein from urea and thermal unfolding curves.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Heat capacity change for ribonuclease A folding.
@en
Heat capacity change for ribonuclease A folding.
@nl
type
label
Heat capacity change for ribonuclease A folding.
@en
Heat capacity change for ribonuclease A folding.
@nl
prefLabel
Heat capacity change for ribonuclease A folding.
@en
Heat capacity change for ribonuclease A folding.
@nl
P2093
P2860
P356
P1433
P1476
Heat capacity change for ribonuclease A folding.
@en
P2093
G I Makhatadze
G R Grimsley
S T Thomas
P2860
P304
P356
10.1110/PS.8.7.1500
P577
1999-07-01T00:00:00Z