[NMR paper] Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Related ArticlesMillisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Angew Chem Int Ed Engl. 2001 Nov 19;40(22):4248-4251
Authors: Wirmer J, Kühn T, Schwalbe H
Abstract
Aspects of the structure of the intermediate populated after 200 ms in the Ca2+ -induced refolding of ?-lactalbumin have been derived by time-resolved photo-CIDNP NMR methods. Refolding at constant denaturant concentration was initiated by laser-induced ion release from photolabile chelators. The NMR data demonstrated that part of the polypeptide chain in the ?-domain of ?-lactalbumin samples adopt non-native conformations while a hydrophobic core of the ?-domain is already formed.
[NMR paper] Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.
Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkout.jstage.jst.go.jp-logo.gif Related Articles Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.
Proc Jpn Acad Ser B Phys Biol Sci. 2017;93(1):10-27
Authors: Nishimura C
Abstract
The structures of apomyoglobin folding intermediates have...
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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] 19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate.
19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate.
19F NMR Studies of a Desolvated Near-Native Protein Folding Intermediate.
Biochemistry. 2013 Aug 1;
Authors: Kitevski-Leblanc JL, Hoang J, Thach W, Larda ST, Prosser RS
Abstract
While many proteins are recognized to undergo folding via an intermediate, the microscopic nature of folding intermediates is less understood. In this study, 19F NMR and near UV circular dichroism (CD) are used to characterize a transition to a thermal folding intermediate of calmodulin, a...
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Real-Time NMR Characterizationof Structure and Dynamicsin a Transiently Populated Protein Folding Intermediate
Real-Time NMR Characterizationof Structure and Dynamicsin a Transiently Populated Protein Folding Intermediate
Enrico Rennella, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge and Bernhard Brutscher
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja302598j/aop/images/medium/ja-2012-02598j_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja302598j
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Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Dmitry M. Korzhnev, Robert M. Vernon, Tomasz L. Religa, Alexandar L. Hansen, David Baker, Alan R. Fersht and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203686t/aop/images/medium/ja-2011-03686t_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203686t
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Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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[NMR paper] Photo-CIDNP NMR methods for studying protein folding.
Photo-CIDNP NMR methods for studying protein folding.
Related Articles Photo-CIDNP NMR methods for studying protein folding.
Methods. 2004 Sep;34(1):75-87
Authors: Mok KH, Hore PJ
Chemically induced dynamic nuclear polarization (CIDNP) is a nuclear magnetic resonance phenomenon that can be used to probe the solvent-accessibility of tryptophan, tyrosine, and histidine residues in proteins by means of laser-induced photochemical reactions, resulting in significant enhancement of NMR signals. CIDNP offers good sensitivity as a surface probe of...
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[NMR paper] Real-time NMR studies on a transient folding intermediate of barstar.
Real-time NMR studies on a transient folding intermediate of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Real-time NMR studies on a transient folding intermediate of barstar.
Protein Sci. 1999 Jun;8(6):1286-91
Authors: Killick TR, Freund SM, Fersht AR
The refolding of barstar, the intracellular...
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
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