Victor Munoz

Affiliations: 
Biochemistry University of Maryland, College Park, College Park, MD 
Area:
General Biophysics, Biochemistry, Bioinformatics Biology
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"Victor Munoz"
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Parents

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Luis Serrano grad student 1995 European Molecular Biology Laboratory (Computational Biology Tree)
William A. Eaton post-doc 1996-2000 NIH
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Publications

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Campos LA, Sadqi M, Muñoz V. (2020) Lessons about Protein Folding and Binding from Archetypal Folds. Accounts of Chemical Research
Nagpal S, Luong TDN, Sadqi M, et al. (2020) Downhill (Un)Folding Coupled to Binding as a Mechanism for Engineering Broadband Protein Conformational Transducers. Acs Synthetic Biology. 9: 2427-2439
Mothi N, Sadqi M, Munoz V. (2020) Catching Fast Protein Folding in the Act: Resolving (Un)Folding Transition Paths using Advanced Single-molecule Spectroscopy Biophysical Journal. 118
Campos LA, Sharma R, Alvira S, et al. (2019) Engineering protein assemblies with allosteric control via monomer fold-switching. Nature Communications. 10: 5703
Szczepaniak M, Iglesias-Bexiga M, Cerminara M, et al. (2019) Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding. Proceedings of the National Academy of Sciences of the United States of America
Campos LA, Sharma R, Alvira S, et al. (2019) Engineering protein assemblies with allosteric control via monomer fold-switching. Nature Communications. 10: 5703-5703
Hashmi A, Sadqi M, Muñoz V. (2019) Engineering a Coiled Coil Protein as pH Sensor Biophysical Journal. 116
Nagpal S, Luong T, Sadqi M, et al. (2019) A Novel Molecular Lego Approach to Measure the Marginal Folding Cooperativity of Intrinsically Disordered Proteins Biophysical Journal. 116
Mothi N, Sadqi M, Munoz V. (2019) Probing (UN)Folding Transition Paths of Fast-Folding Proteins by Single-Molecule Fluorescence: Exploring the Role of Secondary Structure, Fold Topology and Sequence Biophysical Journal. 116
He Y, Nagpal S, Sadqi M, et al. (2018) Glutton: A tool for generating structural ensembles of partly disordered proteins from chemical shifts. Bioinformatics (Oxford, England)
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