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Deficiency of disulfide bonds facilitating fibrillogenesis of endostatinThe Structure of Carbonic Anhydrase IX Is Adapted for Low-pH CatalysisA partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS)Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Characterization of acid-induced unfolding intermediates of glucose/xylose isomerase.Analysis of long-range interactions in a model denatured state of staphylococcal nuclease based on correlated changes in backbone dynamics.Effect of sequential deletion of extra N-terminal residues on the structure and stability of yeast iso-1-cytochrome-c.Toward resolution of ambiguity for the unfolded state.Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.The methanol-induced transition and the expanded helical conformation in hen lysozyme.Differential stability of beta-sheets and alpha-helices in beta-lactamase: a high temperature molecular dynamics study of unfolding intermediates.Ultraviolet Raman examination of the environmental dependence of bombolitin I and bombolitin III secondary structureBackbone dipoles generate positive potentials in all proteins: origins and implications of the effectStructural characterization of the pH-denatured states of ferricytochrome-c by synchrotron small angle X-ray scattering.Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisited.Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthaseHeterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition.The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding.Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetryThe pKa of His-24 in the folding transition state of apomyoglobin.Association-induced folding of globular proteins.Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase.Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease.Urea-induced conformational changes in cold- and heat-denatured states of a protein, Streptomyces subtilisin inhibitorConformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra.Association of partially-folded intermediates of staphylococcal nuclease induces structure and stability.The acid-induced folded state of Sac7d is the native state.Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome cbeta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange.Thermal stability of lysozyme as a function of ion concentration: a reappraisal of the relationship between the Hofmeister series and protein stabilityThe mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome.The role of surface charge in the desolvation process of gelatin: implications in nanoparticle synthesis and modulation of drug releasePurification and biophysical characterization of the CapA membrane protein FTT0807 from Francisella tularensis.Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c.Effects of salt or cosolvent addition on solubility of a hydrophobic solute in water: Relevance to those on thermal stability of a protein.pH-dependent local structure of ferricytochrome c studied by x-ray absorption spectroscopy.Structural characteristics of thermostable immunogenic outer membrane protein from Salmonella enterica serovar Typhi.Elucidation of acid-induced unfolding and aggregation of human immunoglobulin IgG1 and IgG2 Fc.
P2860
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P2860
description
1990 nî lūn-bûn
@nan
1990 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Mechanism of acid-induced folding of proteins.
@ast
Mechanism of acid-induced folding of proteins.
@en
type
label
Mechanism of acid-induced folding of proteins.
@ast
Mechanism of acid-induced folding of proteins.
@en
prefLabel
Mechanism of acid-induced folding of proteins.
@ast
Mechanism of acid-induced folding of proteins.
@en
P2093
P356
P1433
P1476
Mechanism of acid-induced folding of proteins.
@en
P2093
P304
P356
10.1021/BI00466A009
P407
P577
1990-04-01T00:00:00Z