Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding.
about
Green-lighting green fluorescent protein: Faster and more efficient folding by eliminating acis-transpeptide isomerization eventThe primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-ProKinetic traps in lysozyme foldingPlant immunophilins: functional versatility beyond protein maturation.Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICKCis-trans peptide variations in structurally similar proteinsExploring knotting mechanisms in protein folding.Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Ca2+-induced linker transformation leads to a compact and rigid collagen-binding domain of Clostridium histolyticum collagenase.The crystal structure of the cis-proline to glycine variant (P114G) of ribonuclease A.Characterization of secondary amide peptide bond isomerization: thermodynamics and kinetics from 2D NMR spectroscopy.The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M β-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon AcylationPreparation and characterization of a biologically active spin-labeled sea anemone toxin.Identification of the protonation site of gaseous triglycine: the cis-peptide bond conformation as the global minimum.ReviewEquilibrium heat-induced denaturation of chitinase 40 from Streptomyces thermoviolaceusDensity Functional Studies on Secondary Amides: Role of Steric Factors in Cis/Trans Isomerization
P2860
Q27681263-732B5115-94EA-4C46-B0C8-0C717C139949Q27740048-39A56647-D8B3-4192-8373-A668102F5435Q33880768-78DF93DF-6BDB-4BE8-BE3E-EF55F9F4E758Q36115558-EF6CE3D1-ECF7-480A-BECD-077C5BA338DEQ36473985-CD4D2CC6-D4B6-461D-8CC6-53C3C74579D0Q36719015-0F8C87C4-C5B5-40CF-890F-44311997E3F7Q36999820-402FE394-989E-4D1D-9817-1D7D14CF45F0Q37235421-C56D27C0-EA3A-4EA3-9D90-EE678A79CEFFQ37434957-15F39834-6AF7-49C5-9570-CB35AD333478Q41881774-8B9FA6C7-E79D-4EC9-898A-92EC4156C7A9Q42136353-DF06018D-86F1-4F69-BFB5-5DC3576FAC93Q42379531-E4545997-8F81-4695-9958-D895A11BA148Q46521349-CDF3E153-AFE1-4ADA-886C-3F7371901CDDQ50616365-8A342903-43A1-4F91-B229-1E4D93D9EBE3Q56866496-88A22641-F2FB-423D-82D1-C57F14A7F66DQ57752608-738C9FC3-1CE3-4EAB-8CD0-71FBA2D12BFCQ58697386-30DC2D42-10CE-4C3B-841B-FA4EE41A69F8
P2860
Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին 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
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@ast
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@en
type
label
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@ast
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@en
prefLabel
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@ast
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@en
P1476
Non-prolyl cis-trans peptide b ...... otein unfolding and refolding.
@en
P2093
P356
10.1016/S0022-2836(95)80039-5
P407
P577
1995-01-01T00:00:00Z