SITE MENU

FACULTY MENU

 Rachel W. Martin

University of California

4136 Natural Sciences I
 Mail Code: 2025
 Irvine, CA 92697

PHONE: (949) 824-7959
FAX:
E-MAIL: rwmartin@uci.edu

 

Rachel W. Martin
Assistant Professor, Chemistry
School of Physical Sciences
Ph.D., Yale University, 2002, Chemistry
B.S., Arizona State University, 1997, Chemistry
Research Interests
solid-state NMR, protein structure, membrane proteins, physical chemistry, chemical biology

Faculty/lab web:
http://www.probemonkey.com
 
Graduate Programs:
 Chemical Biology
 
 
Abstract
Locally ordered protein networks are biomaterials that have significant short-range order but lack long-range crystallinity. Although these materials are difficult to study because of their compositional heterogeneity, they are central to many interesting biophysical questions. Systems of particular interest include non-crystalline protein aggregates and proteins associated with phospholipid membranes. We develop and use modern solid-state NMR methods to investigate biologically relevant protein networks using the 800 MHz NMR spectrometer at UC Irvine. Graduate students are involved in all aspects of this research, including design and construction of NMR equipment, development of pulse sequences, and preparation of protein and membrane samples. The venom of the male platypus, Ornithorhyncus anatinus, contains several distinct components, including a novel class of defensin-like peptides (DLPs) whose biological function is currently unknown despite structural similarity in solution to known antimicrobial defensins, many of which form pores in membranes. Switched angle spinning (SAS) NMR of macroscopically ordered membrane samples allows us to measure structural and orientational information about membrane associated peptides. As increasing numbers of antibiotic-resistant bacterial strains are discovered, novel antibacterial agents are needed. Even more importantly, this research may lead to a more general understanding of antimicrobial activity in membrane-associated peptide toxins. The eye lens is primarily composed of crystallin proteins that maintain its structure and transparency. Cataracts, which are a major cause of blindness, result when structural crystallins aggregate, causing opacity of the lens. Structural information about the native crystallin oligomers and the aggregates formed when this system breaks down will lead to greater understanding of cataract formation and possibly to future non-surgical interventions.


Other Experience
Updated: Last Updated: 06/10/2009

  C. Qian, P. Thureau, and R.W. Martin. “Variable angle spinning (VAS) experiments for strongly oriented systems: methods development and preliminary results,” Mag. Res. Chem. 46 351-355 (2008).

C. Qian, A. Pines, and R.W. Martin. “Design and construction of a contactless mobile RF coil for double resonance Variable Angle Spinning NMR,” J. Mag. Res. 188 183-189 (2007).

R.C. Jachmann, D.R. Trease, L.S. Bouchard, D. Sakellariou, R.W. Martin, R.D. Schlueter, T.F. Budinger, and A. Pines. “Multipole shimming of permanent magnets using harmonic corrector rings,” Rev. Sci. Inst. 78 (3) Art. No 035115 (2007).

R. W. Martin, R. C. Jachmann, D. Sakellariou, U. G. Nielsen, and A. Pines, "High-resolution NMR spectroscopy of biological tissues using projected magic angle spinning," Magnetic Resonance in Medicine 54; 253-257 (2005).

D. Sakellariou, C. A. Meriles, R. W. Martin, and A. Pines, "NMR in rotating magnetic fields: Magic angle field spinning," Magnetic Resonance Imaging 23 (2); 295-299 (2005).

T. I. Igumenova, A. E. McDermott, K. W. Zilm, R. W. Martin, E. K. Paulson, and A. J. Wand, "Assignments of carbon NMR resonances for microcrystalline ubiquitin," J. Am. Chem. Soc. 126 (21); 6720-6727 (2004).

A. G. Shahkhatuni, A. A. Shakhatuni, H. A. Panosyan, G. H. J. Park, R. W. Martin, and A. Pines, "NMR studies of 13C-iodomethane: Different behavior in thermotropic and lyotropic liquid crystals," J. Phys. Chem. A 108 (33); 6809-6813 (2004).

C. Leal, D. Topgaard, R. W. Martin, and H. Wennerstrom, "NMR studies of molecular mobility in a DNA-amphiphile complex," J. Phys. Chem. B 108; 15392-15397 (2004).

G. H. J. Park, R. W. Martin, D. Sakellariou, A. Pines, A. G. Shahkhatuni, A. A. Shakhatuni, and H. A. Panosyan, "Variable angle spinning (VAS) NMR study of solvent effects in liquid crystalline solutions of 13C-iodomethane," Chem. Phys. Lett. 399; 196-199 (2004).

E. K. Paulson, R. W. Martin, and K. W. Zilm, "Cross-polarization, radio-frequency field homogeneity, and circuit balancing in high-field solid-state NMR probes," Journal of Magnetic Resonance 171; 314-323 (2004).

D. Topgaard, R. W. Martin, D. Sakellariou, C. A. Meriles, and A. Pines, "NMR spectroscopy in an inhomogeneous magnetic field using 'shim pulses'," Proc. Natl. Acad. Sci. USA 101 (51); 17576-17581 (2004).

R. W. Martin and K. W. Zilm, "Variable temperature system using vortex tube cooling and fiber optic temperature sensor for low temperature magic angle spinning NMR," Journal of Magnetic Resonance 168; 202-209 (2004).

D. Sakellariou., C. A. Meriles, R. W. Martin, and A. Pines, "High-resolution NMR of anisotropic samples with spinning away from the magic angle," Chem. Phys. Lett. 377; 333-339 (2003).

R. W. Martin and K. W. Zilm, "Preparation of protein nanocrystals and their characterization by solid-state NMR," Journal of Magnetic Resonance 165; 162-174 (2003).

R. W. Martin, E. K. Paulson, and K. W. Zilm, "Design of a triple resonance magic angle sample spinning probe for high field solid-state nuclear magnetic resonance," Review of Scientific Instruments 74(6); 3045-3061 (2003).

A. McDermott, T. Polenova, A. Bockmann, K. W. Zilm, E. K. Paulson., R. W. Martin, and G. T. Montelione, "Partial NMR assignments for uniformly 13C-15N-enriched BPTI in the solid state," Journal of Biomolecular NMR. 16; 209-219 (2000).
FACULTY