Time-resolved protein activation by proximal decaging in living systems - Nature.com
Time-resolved protein activation by proximal decaging in living systems - Nature.com
Time-resolved protein activation by proximal decaging in living systems Nature.comA universal gain-of-function approach for selective and temporal control of protein activity in living systems is crucial to understanding dynamic cellular ...
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05-09-2019 05:55 AM
[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
<img alt="" height="1" width="1">
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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01-12-2017 03:48 AM
[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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01-12-2017 03:48 AM
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
A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding
A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding
Abstract A 2D 13C Chemical Exchange Saturation Transfer (CEST) experiment is presented for studying slowly exchanging protein systems using methyl groups as probes. The utility of the method is first established through studies of protein L, a small protein, for which chemical exchange on the millisecond time-scale is not observed. Subsequently the approach is applied to a folding exchange reaction of a G48M mutant Fyn SH3 domain, for which only cross-peaks...
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06-16-2012 06:01 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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