Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
about
Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerizationDirect observation of parallel folding pathways revealed using a symmetric repeat protein system.Evidence for involvement of proline cis-trans isomerization in the slow unfolding reaction of RNase A.Toward a better understanding of protein folding pathwaysThe mechanism of self-assembly of the multi-enzyme complex tryptophan synthase from Escherichia coli.Role of proline isomerization in folding of ribonuclease A at low temperaturesGlycoprotein folding in the endoplasmic reticulum.Protein folding: matching theory and experimentGuanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.Structure and stability of the P93G variant of ribonuclease A.Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A.Regeneration of RNase A from the reduced protein: models of regeneration pathways.Folding subdomains of thioredoxin characterized by native-state hydrogen exchangeA general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions.Overview of protein folding mechanisms: experimental and theoretical approaches to probing energy landscapes.Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.Cis proline mutants of ribonuclease A. I. Thermal stability.Protein folding: are we there yet?Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: evidence for two independent reactionsThe problem was to find the problem.A carboxypeptidase Y pulse method to study the accessibility of the C-terminal end during the refolding of ribonuclease A.Molecular basis for proline- and arginine-rich peptide inhibition of proteasome.Trapping the fast-refolding state of ribonuclease A at subzero temperatures.Identification of three phases in Onconase refolding.
P2860
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P2860
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
description
1973 nî lūn-bûn
@nan
1973 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1973 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1973年の論文
@ja
1973年論文
@yue
1973年論文
@zh-hant
1973年論文
@zh-hk
1973年論文
@zh-mo
1973年論文
@zh-tw
1973年论文
@wuu
name
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@ast
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@en
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@nl
type
label
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@ast
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@en
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@nl
prefLabel
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@ast
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@en
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@nl
P2860
P356
P1476
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
@en
P2093
P2860
P304
P356
10.1073/PNAS.70.12.3347
P407
P577
1973-12-01T00:00:00Z