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Arghya Barman, Ph.D.

Affiliations: 
2012 Chemistry University of Miami, Coral Gables, FL 
Area:
Biochemistry, General Biophysics
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"Arghya Barman"
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Parents

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Rajeev Prabhakar grad student 2012 University of Miami
 (Mechanistic and structural studies of proteases, peptidases and amyloid beta peptide: An integrated computational approach.)

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Publications

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Paul TJ, Barman A, Ozbil M, et al. (2016) Mechanisms of peptide hydrolysis by aspartyl and metalloproteases. Physical Chemistry Chemical Physics : Pccp. 18: 24790-24801
Barman A, Hamelberg D. (2016) Coupled Dynamics and Entropic Contribution to the Allosteric Mechanism of Pin1. The Journal of Physical Chemistry. B
Barman A, Smitherman C, Souffrant M, et al. (2016) Conserved Hydration Sites in Pin1 Reveal a Distinctive Water Recognition Motif in Proteins. Journal of Chemical Information and Modeling. 56: 139-47
Barman A, Batiste B, Hamelberg D. (2015) Pushing the Limits of a Molecular Mechanics Force Field To Probe Weak CH···π Interactions in Proteins. Journal of Chemical Theory and Computation. 11: 1854-63
Liu F, Geng J, Gumpper RH, et al. (2015) An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE. The Journal of Biological Chemistry. 290: 15621-34
Zhang T, Ozbil M, Barman A, et al. (2015) Theoretical insights into the functioning of metallopeptidases and their synthetic analogues. Accounts of Chemical Research. 48: 192-200
Barman A, Hamelberg D. (2015) Loss of intramolecular electrostatic interactions and limited conformational ensemble may promote self-association of cis-tau peptide. Proteins. 83: 436-44
Zhang T, Ozbil M, Barman A, et al. (2015) Theoretical insights into the functioning of metallopeptidases and their synthetic analogues Accounts of Chemical Research. 48: 192-200
Barman A, Prabhakar R. (2014) Computational Insights into Substrate and Site Specificities, Catalytic Mechanism, and Protonation States of the Catalytic Asp Dyad of β -Secretase. Scientifica. 2014: 598728
Barman A, Hamelberg D. (2014) Cysteine-mediated dynamic hydrogen-bonding network in the active site of Pin1. Biochemistry. 53: 3839-50
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