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Ashok A. Deniz
Researcher at Scripps Research Institute
Publications - 82
Citations - 7086
Ashok A. Deniz is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Protein folding & Intrinsically disordered proteins. The author has an hindex of 34, co-authored 72 publications receiving 6194 citations. Previous affiliations of Ashok A. Deniz include University of Chicago & Lawrence Berkeley National Laboratory.
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Journal ArticleDOI
Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Förster distance dependence and subpopulations
Ashok A. Deniz,Maxime Dahan,Jocelyn R. Grunwell,Taekjip Ha,Taekjip Ha,Ann Elise Faulhaber,Daniel S. Chemla,Daniel S. Chemla,Shimon Weiss,Peter G. Schultz +9 more
TL;DR: The denaturation of a DNA hairpin was examined by using single-pair FRET to measure intramolecular distances and identify subpopulations of freely diffusing macromolecules in a heterogeneous ensemble.
Journal ArticleDOI
Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism
Taekjip Ha,Alice Y. Ting,Joy Liang,W. Brett Caldwell,Ashok A. Deniz,Daniel S. Chemla,Daniel S. Chemla,Peter G. Schultz,Shimon Weiss +8 more
TL;DR: The experimental methods demonstrated here should prove generally useful in studies of protein folding and enzyme catalysis at single-molecule resolution.
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Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2.
Ashok A. Deniz,Ted A. Laurence,Gangamani S. Beligere,Maxime Dahan,Andrew B. Martin,Daniel S. Chemla,Philip E. Dawson,Peter G. Schultz,Shimon Weiss +8 more
TL;DR: It is shown that new information about different aspects of the protein folding reaction can be extracted from such subpopulation properties, and shifts in the mean transfer efficiencies, FRET efficiency distributions, and denaturation curves are discussed.
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Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence.
TL;DR: The results imply that the 2 folded structures are preencoded by the α-synuclein amino acid sequence, and are tunable by small-molecule supramolecular states and differing membrane properties, suggesting novel control elements for biological and amyloid regulation of α- Synuclein.
Journal ArticleDOI
Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA
Diana M. Mitrea,Jaclyn A Cika,Jaclyn A Cika,Clifford S. Guy,David Ban,Priya R. Banerjee,Christopher B. Stanley,Amanda Nourse,Ashok A. Deniz,Richard W. Kriwacki,Richard W. Kriwacki +10 more
TL;DR: It is shown that nucleophosmin (NPM1) integrates within the nucleolus via a multi-modal mechanism involving multivalent interactions with proteins containing arginine-rich linear motifs (R-motifs) and ribosomal RNA (rRNA), which are found in canonical nucleolar localization signals.