Evans, John Spencer (1993) NMR and computational studies on the conformational folding of the biomineralization template, phosphophoryn. Dissertation (Ph.D.), California Institute of Technology. https://resolver.caltech.edu/Caltech...2009-152426877
Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR [Biophysics and Computational Biology]
Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR
Jakob Maciejko, Jagdeep Kaur, Johanna Becker-Baldus, Clemens Glaubitz...
Date: 2019-04-23
Proteorhodopsin (PR) is a highly abundant, pentameric, light-driven proton pump. Proton transfer is linked to a canonical photocycle typical for microbial ion pumps. Although the PR monomer is able to undergo a full photocycle, the question arises whether the pentameric complex formed in the membrane via specific cross-protomer interactions plays... Read More
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04-23-2019 07:54 PM
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell [Biophysics and Computational Biology]
Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell
Cyril Charlier, T. Reid Alderson, Joseph M. Courtney, Jinfa Ying, Philip Anfinrud, Adriaan Bax...
Date: 2018-05-01
In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins with a substantial volume difference between the folded and unfolded states, their thermodynamic equilibrium can be altered by varying the hydrostatic pressure. Using a pressure-sensitized mutant of ubiquitin, we demonstrate that rapidly switching the...
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05-01-2018 10:57 PM
[NMR paper] Solid-State NMR Studies of Biomineralization Peptides and Proteins.
Solid-State NMR Studies of Biomineralization Peptides and Proteins.
Solid-State NMR Studies of Biomineralization Peptides and Proteins.
Acc Chem Res. 2013 Aug 9;
Authors: Roehrich A, Drobny G
Abstract
Nature has evolved sophisticated strategies for engineering hardtissues through the interaction of proteins, and ultimately cells, with inorganic mineral phases. This process, called biomineralization, is how living organisms transform inorganic materials such as hydroxyapatite, calcite, and silica into highly intricate and organized...
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08-13-2013 04:26 PM
[NMR paper] Structure-activity studies of lGnRH-III through rational amino acid substitution and NMR conformational studies.
Structure-activity studies of lGnRH-III through rational amino acid substitution and NMR conformational studies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Structure-activity studies of lGnRH-III through rational amino acid substitution and NMR conformational studies.
Biopolymers. 2012;98(6):525-34
Authors: Pappa EV, Zompra AA, Diamantopoulou Z, Spyranti Z, Pairas G, Lamari FN, Katsoris P, Spyroulias GA, Cordopatis P
Abstract...
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04-18-2013 10:12 PM
[NMR paper] NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
Related Articles NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
Structure. 2005 Aug;13(8):1193-202
Authors: Arolas JL, D'Silva L, Popowicz GM, Aviles FX, Holak TA, Ventura S
The III-A intermediate constitutes the major rate-determining step in the oxidative folding of leech carboxypeptidase inhibitor...
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12-01-2010 06:56 PM
[NMR paper] Probing site-specific conformational distributions in protein folding with solid-stat
Probing site-specific conformational distributions in protein folding with solid-state NMR.
Related Articles Probing site-specific conformational distributions in protein folding with solid-state NMR.
Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3284-9
Authors: Havlin RH, Tycko R
We demonstrate an experimental approach to structural studies of unfolded and partially folded proteins in which conformational distributions are probed at a site-specific level by 2D solid-state 13C NMR spectroscopy of glassy frozen solutions. Experiments on chemical...
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11-24-2010 11:14 PM
[NMR paper] Folding, conformational changes, and dynamics of cytochromes C probed by NMR spectros
Folding, conformational changes, and dynamics of cytochromes C probed by NMR spectroscopy.
Related Articles Folding, conformational changes, and dynamics of cytochromes C probed by NMR spectroscopy.
Inorg Chem. 2004 Dec 13;43(25):7934-44
Authors: Bren KL, Kellogg JA, Kaur R, Wen X
NMR spectroscopy has become a vital tool for studies of protein conformational changes and dynamics. Oxidized Fe(III)cytochromes c are a particularly attractive target for NMR analysis because their paramagnetism (S = (1)/(2)) leads to high (1)H chemical shift...
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11-24-2010 10:03 PM
[NMR thesis] NMR and computational studies on the conformational folding of the biomineralization
NMR and computational studies on the conformational folding of the biomineralization template, phosphophoryn
Evans, John Spencer (1993) NMR and computational studies on the conformational folding of the biomineralization template, phosphophoryn. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechTHESIS:10212009-152426877
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NMR and computational studies on the conformational folding of the biomineralization template, phosphophoryn
Linear Mode
