Works (4)

Updated: July 5th, 2023 15:54

2011 journal article

Beyond the Random Coil: Stochastic Conformational Switching in Intrinsically Disordered Proteins

STRUCTURE, 19(4), 566–576.

By: U. Choi n, J. McCann*, K. Weninger n & M. Bowen*

TL;DR: Surprisingly, two proteins, neuroligin and the NMDAR-2B glutamate receptor, were observed to stochastically switch among distinct conformational states despite the fact that they appeared intrinsically disordered by other measures. (via Semantic Scholar)
UN Sustainable Development Goal Categories
15. Life on Land (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2010 journal article

Optimizing Methods to Recover Absolute FRET Efficiency from Immobilized Single Molecules

BIOPHYSICAL JOURNAL, 99(3), 961–970.

MeSH headings : Animals; Base Sequence; DNA / chemistry; DNA / genetics; Disks Large Homolog 4 Protein; Fluorescence Resonance Energy Transfer / methods; Immobilized Proteins / chemistry; Intracellular Signaling Peptides and Proteins / chemistry; Membrane Proteins / chemistry; Molecular Sequence Data; Mutant Proteins / chemistry; Photobleaching; Rats; Reference Standards
TL;DR: This is the first systematic study of methods to recover the true FRET efficiency using DNA rulers with known fluorophore separations and per-molecule gamma-normalization was the most effective depending on how it was applied. (via Semantic Scholar)
UN Sustainable Development Goal Categories
7. Affordable and Clean Energy (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2010 journal article

Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 17(3), 318–U84.

By: U. Choi n, P. Strop*, M. Vrljic*, S. Chu*, A. Brunger* & K. Weninger n

MeSH headings : Animals; Calcium / metabolism; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange; Fluorescence Resonance Energy Transfer; Protein Binding; Rats; Recombinant Fusion Proteins / chemistry; Recombinant Fusion Proteins / genetics; Recombinant Fusion Proteins / metabolism; SNARE Proteins / chemistry; SNARE Proteins / genetics; SNARE Proteins / metabolism; Synaptotagmin I / chemistry; Synaptotagmin I / genetics; Synaptotagmin I / metabolism
TL;DR: An experimentally determined model of the elusive Syt1–SNARE complex is obtained using a multibody docking approach with 34 FRET-derived distances as restraints, suggesting a common mechanism by which the interaction between synaptotagmins and SNAREs aids in Ca2+-triggered fusion. (via Semantic Scholar)
UN Sustainable Development Goal Categories
7. Affordable and Clean Energy (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2008 journal article

Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1 : 1 syntaxin/SNAP-25 complex

STRUCTURE, 16(2), 308–320.

MeSH headings : Fluorescence Resonance Energy Transfer; Lipid Bilayers / metabolism; Protein Structure, Tertiary; Qa-SNARE Proteins / chemistry; Qa-SNARE Proteins / metabolism; R-SNARE Proteins / metabolism; SNARE Proteins / metabolism; Synaptosomal-Associated Protein 25 / chemistry; Synaptosomal-Associated Protein 25 / metabolism
TL;DR: The structure of the 1:1 syntaxin/SNAP-25 binary complex is variable, with states changing on the second timescale, and one state corresponds to a parallel three-helix bundle, whereas other states show one of the SNAP-25 SNARE domains dissociated. (via Semantic Scholar)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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