Dr. Richard Harris     Associate, Department of Biochemistry      FORCHHEIMER BLDG.- ROOM 303      Tel: 718 430-2021      Email: rharris@medusa.bioc.aecom.yu.edu

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My newly created position at Einstein is to provide non-NMR groups with access to expertise in NMR spectroscopy as applied to functional and structural studies of biological systems.


NMR spectroscopy is mostly applied to the study of proteins of less than 100kD and could involve structural work, understanding protein dynamics or interactions of proteins with ligands - with other proteins, dna or small molecules. Although studies on RNA/DNA and carbohydrates are also possible.


My particular forte is in solving three dimensional solution structures, which I became involved in during my time at University College London, and recently I solved my first structure at Einstein - a 73 amino acid homoedomain. Below are examples of some of the proteins I have worked on along with selected references.


If you are interested in finding out more about whether NMR could be applicable to you research then please contact me (details above).

Selected Solution Structures solved:

Homeodomain solved at AECOM	Prod1	PLC epsilon 2nd Ras Association  domain
PLC gamma2 split Pleckstrin Homology domain	VirB7/9 complex	C-terminal domain of Ku80

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Selected References (full listing)


1. “Solution structure and phylogenetics of Prod1, a member of the three-finger protein superfamily implicated in Salamander limb regeneration." (2009). PloS ONE, 4 (9), e7123
   A. Garza-Garcia, R. Harris, D. Esposito, P.B. Gates and P.C. Driscoll.
   

2. “rac regulates its effector phospholipase Cgamma2 through interaction with a split pleckstrin homology domain.” (2008). J. Biol. Chem., 283 (44), p30351-30362.
   C. Walliser, M. Retlich, R. Harris, K.L. Everett, M.B. Josephs, P.Vatter, D. Esposito, P.C. Driscoll, M. Katan, P. Gierschik and T.D. Bunney.
   

3. “Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b.” (2008). J. Mol. Biol., 379, p981-990.
   P. Patel, R. Harris, S.M. Geddes, E.M. Strehle, J.D. Watson, R. Bashir, K. Bushby, P.C. Driscoll and N.H. Keep.

4. “Three-dimensional solution structure and conformational plasticity of the N-terminal scavenger receptor cysteine-rich domain of human CD5.” (2008). J. Mol. Biol., 378 (1), p129-144.
   A. Garza-Garcia, D. Esposito, W. Rieping, R. Harris, C. Briggs, M.H. Brown and P.C. Driscoll.

5. “NMR structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system.”(2007). PNAS, 104 (5), p1673-1678.
   R. Bayliss, R. Harris, L. Coutte, A. Monier, R. Fronzes, P.J. Christie, P.C. Driscoll and G. Waksman.

6. “Structural and mechanistic insights into ras association domains of phospholipase Cε.” (2005). Mol. Cell, 21 (4), p495-507.
   T.D. Bunney, R. Harris, N.L. Gandarillas, M.B. Josephs, S.M. Roe, H.F. Paterson, F. Rodrigues-Lima, D. Esposito, P. Gierschik, L.H. Pearl, P.C. Driscoll and M. Katan

7. “The 3D solution structure of the C-terminal region of Ku86 (Ku86CTR).” (2004). J. Mol. Biol., 335, p573-582.
   R. Harris, D. Esposito, A. Sankar, J.D. Maman, J.A. Hinks, L.H. Pearl and P.C. Driscoll.

8. “Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide” (2003). Biophys. J., 84, p185-194.
   T.P. Galbraith, R. Harris, P.C. Driscoll and B.A. Wallace.

9. “Stable isotope assisted NMR studies on ¹³C-enriched sialyl Lewis^X in solution and bound to E-selectin.” (1999). J. Am. Chem. Soc.121, p2546-2551.
   R. Harris, G.R. Kiddle, R.A. Field, M.J. Milton, B. Ernst, J.L. Magnani and S. W. Homans.





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File Updated 11/2009