[NMR paper] Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.
Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.
Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.
Sci Adv. 2015 Dec;1(11):e1501087
Authors: Shi C, Fricke P, Lin L, Chevelkov V, Wegstroth M, Giller K, Becker S, Thanbichler M, Lange A
Abstract
Bactofilins are a recently discovered class of cytoskeletal proteins of which no atomic-resolution structure has been reported thus far. The bacterial cytoskeleton plays an essential role in a wide range of processes, including...
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12-15-2015 08:09 PM
[NMR paper] Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.
Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.
Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.
Proc Natl Acad Sci U S A. 2015 Nov 24;112(47):14611-6
Authors: Yan S, Guo C, Hou G, Zhang H, Lu X, Williams JC, Polenova T
Abstract
Microtubules and their associated proteins perform a broad array of essential physiological functions, including...
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11-26-2015 12:22 PM
De novo protein structure determination from near-atomic-resolution cryo-EM maps - Nature.com
De novo protein structure determination from near-atomic-resolution cryo-EM maps - Nature.com
<img alt="" height="1" width="1">
De novo protein structure determination from near-atomic-resolution cryo-EM maps
Nature.com
Despite these developments, little progress has been made in de novo model building into near-atomic-resolution cryo-EM density maps. Structural interpretation of cryo-EM maps typically starts with fitting an atomic X-ray or NMR structure into the map5.
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02-24-2015 02:48 PM
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
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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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...