Prolyl cis/trans isomerization is a rate-limiting step in protein folding, often coupling directly to the acquisition of native structure. Here, we investigated the interplay between folding and prolyl isomerization in the N2 domain of the gene-3-protein from filamentous phage fd, which adopts a native-state cis/trans equilibrium at Pro161. Using mutational and ?-value analysis, we identified a discrete folding nucleus encompassing the ?-strands surrounding Pro161. These native-like interactions...
[NMR paper] Proline Peptide Bond Isomerization in Ubiquitin under Folding and Denaturing Conditions by Pressure-Jump NMR
Proline Peptide Bond Isomerization in Ubiquitin under Folding and Denaturing Conditions by Pressure-Jump NMR
Proline isomerization is widely recognized as a kinetic bottleneck in protein folding, amplified for proteins rich in Pro residues. We introduced repeated hydrostatic pressure jumps between native and pressure-denaturing conditions inside an NMR sample cell to study proline isomerization in the pressure-sensitized L50A ubiquitin mutant. Whereas in two unfolded heptapeptides, X-Pro peptide bonds isomerized ca 1.6-fold faster at 1 bar than at 2.5 kbar, for ubiquitin ca eight-fold...
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[NMR paper] Including the Ensemble of Unstructured Conformations in the Analysis of Protein's Native State by High-Pressure NMR Spectroscopy
Including the Ensemble of Unstructured Conformations in the Analysis of Protein's Native State by High-Pressure NMR Spectroscopy
The analysis of pressure induced changes in the chemical shift of proteins allows statements on structural fluctuations proteins exhibit at ambient pressure. The inherent issue of separating general pressure effects from structural related effects on the pressure dependence of chemical shifts has so far been addressed by considering the characteristics of random coil peptides on increasing pressure. In this work, chemically and pressure denatured states of the...
The Non-native Helical Intermediate State May Accumulateat Low pH in the Folding and Aggregation Landscape of the IntestinalFatty Acid Binding Protein
The Non-native Helical Intermediate State May Accumulateat Low pH in the Folding and Aggregation Landscape of the IntestinalFatty Acid Binding Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00390/20160803/images/medium/bi-2016-003902_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00390
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[NMR paper] Structural Analysis of N- and O-glycans Using ZIC-HILIC/DIALYSIS Coupled to NMR Detection.
Structural Analysis of N- and O-glycans Using ZIC-HILIC/DIALYSIS Coupled to NMR Detection.
Related Articles Structural Analysis of N- and O-glycans Using ZIC-HILIC/DIALYSIS Coupled to NMR Detection.
Fungal Genet Biol. 2014 Aug 9;
Authors: Qu Y, Feng J, Deng S, Cao L, Zhang Q, Zhao R, Zhang Z, Jiang Y, Zink EM, Baker SE, Lipton MS, Paša-Toli? L, Hu JZ, Wu S
Abstract
Protein glycosylation, an important and complex post-translational modification (PTM), is involved in various biological processes, including the receptor-ligand and...
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08-15-2014 12:53 PM
[NMR paper] Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
Gradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR.
J Phys Chem B. 2013 Jun 24;
Authors: Campos LA, Sadqi M, Liu J, Wang X, English DS, Munoz V
Abstract
Theory predicts that folding free energy landscapes are intrinsically malleable, and as such are expected to respond to perturbations in topographically complex...
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06-27-2013 01:52 AM
[NMR paper] Structural analysis of non-native states of proteins by NMR methods.
Structural analysis of non-native states of proteins by NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural analysis of non-native states of proteins by NMR methods.
Curr Opin Struct Biol. 1996 Feb;6(1):24-30
Authors: Shortle DR
Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist...
Phi-Value and NMR Structural Analysis of a Coupled Native-State Prolyl Isomerization and Conformational Protein Folding Process
Hybrid Mode
