Reexamination of the folding of BPTI: predominance of native intermediates.
about
Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulumReactivity of thioredoxin as a protein thiol-disulfide oxidoreductaseMacromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cellGraph-representation of oxidative folding pathwaysDisulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotidesThe NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathwaysDeciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase InhibitorSynergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein foldingStructural plasticity of 4- -helical bundles exemplified by the puzzle-like molecular assembly of the Rop proteinSynthesis and characterization of the sweet protein brazzeinDifferential cooperative enzymatic activities of protein disulfide isomerase family in protein folding.Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitorDisulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.Oxidative folding of Amaranthus alpha-amylase inhibitor: disulfide bond formation and conformational folding.Hydrogen exchange in BPTI variants that do not share a common disulfide bond.Principles of protein folding--a perspective from simple exact models.Molecular force modulation spectroscopy revealing the dynamic response of single bacteriorhodopsins.A major kinetic trap for the oxidative folding of human epidermal growth factor.Hierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase.Mutations in the N- and C-terminal tails of potato carboxypeptidase inhibitor influence its oxidative refolding process at the reshuffling stage.Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry.Characterization of peptide folding nuclei by hydrogen/deuterium exchange-mass spectrometry.Kinetic traps in lysozyme foldingThermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trappingComplete pathway for protein disulfide bond formation encoded by poxvirusesMechanism of phage P22 tailspike protein folding mutations.Structural determinants of oxidative folding in proteinsDifferent interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitorFrustration in biomoleculesHigh throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli.Denaturation and unfolding of human anaphylatoxin C3a: an unusually low covalent stability of its native disulfide bondsProtein folding as a complex reaction: a two-component potential for the driving force of folding and its variation with folding scenario.Salt-induced detour through compact regions of the protein folding landscapePreferential binding of an unfolded protein to DsbA.Protein folding guides disulfide bond formationCooperativity in protein-folding kinetics.An entropy criterion to detect minimally frustrated intermediates in native proteins.Denaturants can accelerate folding rates in a class of globular proteins.Mutational analysis of the BPTI folding pathway: I. Effects of aromatic-->leucine substitutions on the distribution of folding intermediates
P2860
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P2860
Reexamination of the folding of BPTI: predominance of native intermediates.
description
1991 nî lūn-bûn
@nan
1991 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Reexamination of the folding of BPTI: predominance of native intermediates.
@ast
Reexamination of the folding of BPTI: predominance of native intermediates.
@en
type
label
Reexamination of the folding of BPTI: predominance of native intermediates.
@ast
Reexamination of the folding of BPTI: predominance of native intermediates.
@en
prefLabel
Reexamination of the folding of BPTI: predominance of native intermediates.
@ast
Reexamination of the folding of BPTI: predominance of native intermediates.
@en
P356
P1433
P1476
Reexamination of the folding of BPTI: predominance of native intermediates.
@en
P2093
P304
P356
10.1126/SCIENCE.1716783
P407
P577
1991-09-01T00:00:00Z