The purpose of the 'Administrative Core'is as follows: (1) provide overall scientific and administrative management of the Program Project;(2) schedule, organize, and run the yearly meeting of the Program Project;(3) schedule travel for PIs/postdocs/students to go from one of the two performance sites to the other in order to conduct research;(4) organize the functions of the External Advisory Committee;and (5) develop, organize, and oversee the web site of the Program Project.

Public Health Relevance

Our studies are aimed at determining the elements of protein structure that create specific dynamics important for catalytic mechanism. We will understand design features that either up or down regulate enzymatic activity. The goal of this research is to lay a foundation for the development and rational design of 'allosteric'effectors or active site inhibitors based on dynamics.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
2P01GM068036-11
Application #
8722197
Study Section
Special Emphasis Panel (ZRG1-VH-F (40))
Project Start
Project End
Budget Start
2014-08-15
Budget End
2015-04-30
Support Year
11
Fiscal Year
2014
Total Cost
$73,764
Indirect Cost
$29,594
Name
Albert Einstein College of Medicine
Department
Type
DUNS #
110521739
City
Bronx
State
NY
Country
United States
Zip Code
10461
Zoi, Ioanna; Antoniou, Dimitri; Schwartz, Steven D (2017) Incorporating Fast Protein Dynamics into Enzyme Design: A Proposed Mutant Aromatic Amine Dehydrogenase. J Phys Chem B 121:7290-7298
Deng, Hua; Vedad, Jayson; Desamero, Ruel Z B et al. (2017) Difference FTIR Studies of Substrate Distribution in Triosephosphate Isomerase. J Phys Chem B 121:10036-10045
Khrapunov, Sergei; Chang, Eric; Callender, Robert H (2017) Thermodynamic and Structural Adaptation Differences between the Mesophilic and Psychrophilic Lactate Dehydrogenases. Biochemistry 56:3587-3595
Eismin, Ryan J; Munusamy, Elango; Kegel, Laurel L et al. (2017) Evolution of Aggregate Structure in Solutions of Anionic Monorhamnolipids: Experimental and Computational Results. Langmuir 33:7412-7424
Peng, Huo-Lei; Callender, Robert (2017) Mechanistic Analysis of Fluorescence Quenching of Reduced Nicotinamide Adenine Dinucleotide by Oxamate in Lactate Dehydrogenase Ternary Complexes. Photochem Photobiol 93:1193-1203
Davis, Caitlin M; Reddish, Michael J; Dyer, R Brian (2017) Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics. Spectrochim Acta A Mol Biomol Spectrosc 178:185-191
Reddish, Michael J; Callender, Robert; Dyer, R Brian (2017) Resolution of Submillisecond Kinetics of Multiple Reaction Pathways for Lactate Dehydrogenase. Biophys J 112:1852-1862
Zoi, Ioanna; Antoniou, Dimitri; Schwartz, Steven D (2017) Electric Fields and Fast Protein Dynamics in Enzymes. J Phys Chem Lett 8:6165-6170
Munusamy, Elango; Luft, Charles M; Pemberton, Jeanne E et al. (2017) Structural Properties of Nonionic Monorhamnolipid Aggregates in Water Studied by Classical Molecular Dynamics Simulations. J Phys Chem B 121:5781-5793
Brás, Natércia F; Fernandes, Pedro A; Ramos, Maria J et al. (2017) Mechanistic Insights on Human Phosphoglucomutase Revealed by Transition Path Sampling and Molecular Dynamics Calculations. Chemistry :

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