This application requests continued support for a Ph.D. Training Program in Molecular Biophysics, which is currently in its tenth year of existence. The training faculty in this proposal primarily have appointments in two closely allied departments, Biochemistry and Physiology & Biophysics. Through required and elective courses, participation in research seminars and discussion groups and, most importantly, through individual research, the student trainees develop the technical skills and critical ability necessary to conduct independent research in Molecular Biophysics. Training consists of three to four years of individual research, often with joint mentoring, after a first year that consists entirely of coursework and laboratory rotations. Both the course work and research training of each student are closely monitored by the Steering Committee for the program. The cohesiveness of the program is assured by regular meetings of the training faculty and trainees under the guidance of the Steering Committee as well as by Core courses taken by all trainees. This program provides valuable training opportunities for students in Molecular Biophysics due to the outstanding faculty and facilities that exist at the Institution In two areas in particular, the program provides unparalleled opportunities. These include synchrotron and laser spectroscopy research. Beamline facilities operated by the College of Medicine at the National Synchrotron Light Source include student access to state-of-the art protein crystallography, x-ray absorption spectroscopy x-ray footprinting, and infrared microspectroscopy techniques. Also, the laser facilities of the College include several laboratories with state-of-the art femtosecond to microsecond time-resolved instrumentation for the study of protein folding and dynamics for student research. The research areas that are especially strong in the trainer's laboratories are Structural Biology, including macromolecular NMR and crystallography time-resolved investigations of protein and nucleic acid folding and protein dynamics; structure function relationships of metalloproteins, metalloenzymes, and enzymes; and allostenc interactions of macromolecules The two departments involved in this proposal are currently attracting excellent trainee candidates and have trained numerous students in the past who have excellent outcomes. The program currently provides training for six pre-doctoral students in each year; this proposal suggests an increase to seven slots per year. ? ?

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM008572-12
Application #
7084524
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Program Officer
Flicker, Paula F
Project Start
1995-07-01
Project End
2010-06-30
Budget Start
2006-07-01
Budget End
2007-06-30
Support Year
12
Fiscal Year
2006
Total Cost
$344,201
Indirect Cost
Name
Albert Einstein College of Medicine
Department
Physiology
Type
Schools of Medicine
DUNS #
110521739
City
Bronx
State
NY
Country
United States
Zip Code
10461
Nicholas, Matthew P; Berger, Florian; Rao, Lu et al. (2015) Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains. Proc Natl Acad Sci U S A 112:6371-6
Hayden, Eric Y; Kaur, Prerna; Williams, Thomas L et al. (2015) Heme Stabilization of ?-Synuclein Oligomers during Amyloid Fibril Formation. Biochemistry 54:4599-610
Nicholas, Matthew P; Rao, Lu; Gennerich, Arne (2014) An improved optical tweezers assay for measuring the force generation of single kinesin molecules. Methods Mol Biol 1136:171-246
Nicholas, Matthew P; Rao, Lu; Gennerich, Arne (2014) Covalent immobilization of microtubules on glass surfaces for molecular motor force measurements and other single-molecule assays. Methods Mol Biol 1136:137-69
Stewart, Alex; Harrison, Joseph S; Regula, Lauren K et al. (2013) Side chain requirements for affinity and specificity in D5, an HIV-1 antibody derived from the VH1-69 germline segment. BMC Biochem 14:9
Harrison, Joseph S; Higgins, Chelsea D; O'Meara, Matthew J et al. (2013) Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteins. Structure 21:1085-96
Fairman, James W; Dautin, Nathalie; Wojtowicz, Damian et al. (2012) Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. Structure 20:1233-43
Capece, Luciana; Lewis-Ballester, Ariel; Yeh, Syun-Ru et al. (2012) Complete reaction mechanism of indoleamine 2,3-dioxygenase as revealed by QM/MM simulations. J Phys Chem B 116:1401-13
Harrison, Joseph S; Koellhoffer, Jayne F; Chandran, Kartik et al. (2012) Marburg virus glycoprotein GP2: pH-dependent stability of the ectodomain ?-helical bundle. Biochemistry 51:2515-25
Udho, Eshwar; Jakes, Karen S; Finkelstein, Alan (2012) TonB-dependent transporter FhuA in planar lipid bilayers: partial exit of its plug from the barrel. Biochemistry 51:6753-9

Showing the most recent 10 out of 27 publications