Proteins often undergo large-scale conformational transitions, in which secondary and tertiary structure elements (loops, helices, and domains) change their structures or their positions with respect to each other. Simple considerations suggest that such dynamics should be relatively fast, but the functional cycles of many proteins are often relatively slow. Sophisticated experimental methods are starting to tackle this dichotomy and shed light on the contribution of large-scale conformational...
[ASAP] Dissecting the Protein Dynamics Coupled Ligand Binding with Kinetic Models and Single-Molecule FRET
Dissecting the Protein Dynamics Coupled Ligand Binding with Kinetic Models and Single-Molecule FRET
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00771/20220228/images/medium/bi1c00771_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00771
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[ASAP] Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
Samuel Naudi-Fabra, Maud Tengo, Malene Ringkjbing Jensen, Martin Blackledge, and Sigrid Milles
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c06264/20211124/images/medium/ja1c06264_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c06264
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[NMR paper] Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS
Studying the conformational landscape of intrinsically disordered and partially folded proteins is challenging and only accessible to a few solution state techniques, such as nuclear magnetic resonance (NMR), small-angle scattering techniques, and single-molecule Förster resonance energy transfer (smFRET). While each of the techniques is sensitive to different properties of the disordered chain, such as local structural propensities, overall dimension, or intermediate- and long-range...
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[ASAP] Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET
Conformational Ensembles of an Intrinsically Disordered Protein Consistent with NMR, SAXS, and Single-Molecule FRET
Gregory-Neal W. Gomes, Mickae?l Krzeminski, Ashley Namini, Erik W. Martin, Tanja Mittag, Teresa Head-Gordon, Julie D. Forman-Kay, and Claudiu C. Gradinaru
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c02088/20200904/images/medium/ja0c02088_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c02088
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[NMR paper] Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
Related Articles Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET.
J Am Chem Soc. 2020 Aug 25;:
Authors: Gomes GW, Krzeminski M, Namini A, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC
Abstract
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging,...
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08-26-2020 02:46 PM
[NMR paper] Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-molecule force spectroscopy (SMFS) has become a powerful tool in investigating the mechanical unfolding/folding of proteins at the single-molecule level. Polyproteins made of tandem identical repeats have been widely used in atomic force microscopy (AFM)-based SMFS studies, where polyproteins not only serve as fingerprints to identify single-molecule stretching events, but may also improve statistics of data...
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12-27-2016 11:04 PM
[NMR paper] Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.
Proc Natl Acad Sci U S A. 2016 Aug 26;
Authors: Aznauryan M, Delgado L, Soranno A, Nettels D, Huang JR, Labhardt AM, Grzesiek S, Schuler B
Abstract
The properties of unfolded proteins are essential both for the mechanisms of protein folding and for the function of the large...
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08-28-2016 11:03 AM
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Methods Enzymol. 2011;493:21-60
Authors: Acton TB, Xiao R, Anderson S, Aramini J, Buchwald WA, Ciccosanti C, Conover K, Everett J, Hamilton K, Huang YJ, Janjua H, Kornhaber G, Lau J, Lee DY, Liu G, Maglaqui M, Ma L, Mao L, Patel D, Rossi P, Sahdev S, Shastry R, Swapna GV, Tang Y, Tong S, Wang D, Wang H, Zhao L, Montelione GT
In this chapter, we...
NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function
Linear Mode
