Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates.
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Structural events during the refolding of an all beta-sheet protein.The perturbations of the native state of goat alpha-lactalbumin induced by 1,1'-bis(4-anilino-5-naphthalenesulfonate) are Ca2+-dependentPertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.Protein antioxidant response to the stress and the relationship between molecular structure and antioxidant function.Protein painting reveals solvent-excluded drug targets hidden within native protein-protein interfaces.HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: structural and functional aspects.Under pressure that splits a family in two. The case of lipocalin familyDeciphering structural intermediates and genotoxic fibrillar aggregates of albumins: a molecular mechanism underlying for degenerative diseases.Biophysical characterization of proteins in the post-genomic era of proteomics.Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform.Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies.Hydrophobic photolabeling as a new method for structural characterization of molten globule and related protein folding intermediates.Early events in protein folding explored by rapid mixing methods.Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulationsRole of individual disulfide bonds in hen lysozyme early folding steps.Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysisConformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c.Structural basis for cyclodextrins' suppression of human growth hormone aggregation.Antiferritin single-chain antibody: a functional protein with incomplete folding?Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies.Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone ProteinsPolyubiquitin Drives the Molecular Interactions of the NF-κB Essential Modulator (NEMO) by Allosteric Regulation.Opposite behavior of two isozymes when refolding in the presence of non-ionic detergentsRefolding of urea-denatured adenylate kinase.Structural and thermodynamic effects of ANS binding to human interleukin-1 receptor antagonist.Inducing toxicity by introducing a leucine-zipper-like motif in frog antimicrobial peptide, magainin 2.Compactness of the kinetic molten globule of bovine alpha-lactalbumin: a dynamic light scattering study.A structure-toxicity study of Aß42 reveals a new anti-parallel aggregation pathway.A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability.Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation.Stepwise proteolytic removal of the beta subdomain in alpha-lactalbumin. The protein remains folded and can form the molten globule in acid solution.The refolding of type II shikimate kinase from Erwinia chrysanthemi after denaturation in urea.Biophysical insight reveals tannic acid as amyloid inducer and conformation transformer from amorphous to amyloid aggregates in Concanavalin A (ConA).The identification of a minimal dimerization motif QXXS that enables homo- and hetero-association of transmembrane helices in vivo.Glyoxal induced structural transition of buffalo kidney cystatin to molten globule and aggregates: Anti-fibrillation potency of quinic acid.Unfolding of diphtheria toxin. Identification of hydrophobic sites exposed on lowering of pH by photolabeling.Molten globule state of human placental cystatin (HPC) at low pH conditions and the effects of trifluoroethanol (TFE) and methanol.Molten globule-like partially folded state of Bacillus licheniformis α-amylase at low pH induced by 1,1,1,3,3,3-hexafluoroisopropanol.Acarbose and the thermal aggregation ofBacillus amyloliquefaciensalpha-amylase (BAA): protective effect of an inhibitor
P2860
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P2860
Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates.
description
1995 nî lūn-bûn
@nan
1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Kinetics of interaction of par ...... n early folding intermediates.
@ast
Kinetics of interaction of par ...... n early folding intermediates.
@en
type
label
Kinetics of interaction of par ...... n early folding intermediates.
@ast
Kinetics of interaction of par ...... n early folding intermediates.
@en
prefLabel
Kinetics of interaction of par ...... n early folding intermediates.
@ast
Kinetics of interaction of par ...... n early folding intermediates.
@en
P2860
P356
P1433
P1476
Kinetics of interaction of par ...... n early folding intermediates.
@en
P2093
M Engelhard
P2860
P304
P356
10.1002/PRO.5560040813
P577
1995-08-01T00:00:00Z