Immunology graduate students in lab The Immunology Graduate Program

L. Mario Amzel, Ph.D.
Professor, Department of Medicine

Johns Hopkins University School of Medicine
Woods Basic Science Building, Rm. 615
725 N. Wolfe St.
Baltimore, Maryland 21205

Office Phone: (410) 955-4735
Fax: (410) 955-9124
Email: mario@neruda.med.jhmi.edu
Lab website: Unavailable/None




Methodologies
X-ray Diffraction. Molecular Modeling. Thermodynamics. Calculations.

Structure of Thermodynamics of Ligand Recognition
Systems are being developed for studying and the structural energetics of ligand recognition. The structures of ligand complexes in four systems were determined and methods are being developed for the quantitative estimation of thermodynamical parameters of binding. The combined use of x-ray diffraction, calorimetry, and combinatorial peptide libraries are providing clues for the design of high affinity ligands.

Phosphoryl Transfers
The structure of Mitochondrial F1-ATPase was determined and is being used to gain insight into the mechanisms of ATP-synthesis and ATP-hydrolysis. The structure and mechanism of Nudix hydrolases is being studied.

Structure and Mechanism of Oxidation/Reduction Enzymes
The structure and mechanism of three enzymes - lipoxygenase, quinone reductase, and peptidylglycine hydroxylating monooxygenase - are being investigated. The three enzymes are targets for the design of therapeutic compounds.

Gabelli SB, McLellan JS, Montalvetti A, Oldfield E, Docampo R, Amzel LM. (2006) Structure and mechanism of the farnesyl diphosphate synthase from Trypanosoma cruzi: implications for drug design. Proteins 8:793-800 [PubMed]

Amzel LM, Siebert X, Armstrong A, Pabon G. (2005) Thermodynamic calculations in biological systems. Biophys Chem 2:269-274 [PubMed]

Vega S, Kang LW, Velazquez-Campoy A, Kiso Y, Amzel LM, Freire E.. (2004) A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease. Proteins 6:283-289 [PubMed]

Kang LW, Gabelli SB, Cunningham JE, O'Handley SF, Amzel LM. (2003) Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis. Structure 155:1293-1302 [PubMed]

Armstrong AA, Amzel LM. (2003) Role of entropy in increased rates of intramolecular reactions. J Am Chem Soc 104:2369 [PubMed]

Announcements
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DateNews
1/11/07Thesis Committee/Oral Exam Update!
8/23/06Webpage Re-launch
8/16/06New Feature
8/13/06New Feature
8/11/06Content Update

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