Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
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Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsEnergetics and mechanisms of folding and flipping the myristoyl switch in the {beta}-trefoil protein, hisactophilinMultiple routes lead to the native state in the energy landscape of the beta-trefoil familyNonnative interactions regulate folding and switching of myristoylated protein.Influence of the valine zipper region on the structure and aggregation of the basic leucine zipper (bZIP) domain of activating transcription factor 5 (ATF5).Conserved and nonconserved features of the folding pathway of hisactophilin, a beta-trefoil protein.Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds.Sonication of proteins causes formation of aggregates that resemble amyloid.Calorimetric analysis of thermodynamic stability and aggregation for apo and holo amyotrophic lateral sclerosis-associated Gly-93 mutants of superoxide dismutase.
P2860
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P2860
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
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name
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
@en
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
@nl
type
label
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
@en
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
@nl
prefLabel
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
@en
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
@nl
P2093
P356
P1433
P1476
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein
@en
P2093
P304
P356
10.1021/BI002609I
P407
P577
2001-04-01T00:00:00Z