[NMR paper] Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Related Articles Millisecond 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...
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05-03-2018 06:46 PM
Tackling Infectious Disease, One Protein at a Time - Infection Control Today
Tackling Infectious Disease, One Protein at a Time - Infection Control Today
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcSxQAQXF8Owx8hxW3zy9QmIb0u7KjyXApANQ9a5LTmgklzhuP7WY99jrVNsDJgqH2MswkZqNTUL
Infection Control Today
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Tackling Infectious Disease, One Protein at a Time
Infection Control Today
A protein in the micro-organism that causes giardiasis, which translates to nausea, abdominal pain, fatigue and other symptoms in hundreds of millions of ...
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06-09-2017 09:13 AM
ProbingConformational Exchange Dynamics in a Short-LivedProtein Folding Intermediate by Real-Time Relaxation–DispersionNMR
ProbingConformational Exchange Dynamics in a Short-LivedProtein Folding Intermediate by Real-Time Relaxation–DispersionNMR
Re?mi Franco, Sergio Gil-Caballero, Isabel Ayala, Adrien Favier and Bernhard Brutscher
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b12089/20170111/images/medium/ja-2016-12089u_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b12089
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/pEuEi5v6HRE
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[NMR paper] Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
J Am Chem Soc. 2017 Jan 11;:
Authors: Franco R, Gil-Caballero S, Ayala I, Favier A, Brutscher B
Abstract
NMR spectroscopy is a powerful tool for studying...
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NMR protein structures: No deuteration required - Physics Today
NMR protein structures: No deuteration required - Physics Today
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NMR protein structures: No deuteration required
Physics Today
Unlike x-ray crystallography, it doesn't require a crystalline sample, and it's well suited to the small and medium-sized membrane proteins currently beyond the reach of cryoelectron microscopy. Even with magic-angle spinning, 1H NMR protein spectra ...
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08-19-2016 04:05 AM
[NMR paper] Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Related Articles Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation.
Anal Chem. 2003 Feb 15;75(4):956-60
Authors: Kakuta M, Jayawickrama DA, Wolters AM, Manz A, Sweedler JV
Time-resolved NMR spectroscopy is used to studychanges in protein conformation based on the elapsed time after a change in the solvent composition of a protein solution. The use of a micromixer and a continuous-flow method is described where the contents of...
Time-resolved NMR probes the dynamics of protein folding - Physics Today
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