Research group of Ann McDermott

Below is a description of research projects of Dr. <SPAN class=FacultyName>McDermott from her departmental web page.

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Research Summary</SPAN>
<P xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">NMR Structural Studies of Membrane Proteins: Most membrane-bound proteins are structurally uncharacterized at present; solid state NMR methods promise to offer important information for these systems. Recently we discovered that NMR spectra of uniformly labeled solid state proteins are well-resolved and may provide the basis for structural and functional studies. Many small proteins, including BPTI and ubiquitin, and several intrinsic membrane proteins have been studied using high-field state-of-the-art solid state NMR equipment. Torsional angles and tertiary contacts are characterized through existing dipolar methods.</P><P xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">Enzymes, Hydrogen Bonding Geometry, and Dynamics: For most enzymes and drug targets, ligand binding is associated with the motion of a flexible loop or domain and the restructuring of hydrogen bonds and other contacts. The characteristic timescales of an active-site flexible loop in TIM is under investigation. Similarly, metal-substrate geometry as well as conformational exchange rates are studied for metalloenzymes, such as the important drug target cytochrome P450. NMR measurements in the active sites of enzymes give insight into catalytic mechanism, drug binding modes, and dynamics.</P><P xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">NMR Methods Development, Enhanced Signals, and Alignment Protocols: NMR signals associated with the photosynthetic apparatus appear with intensities enhanced 300 to 1,000 times, relative to control values. We have proposed a mechanism for this remarkable effect and achieved quantitative agreement. We have demonstrated alignment of liquids in the presence of large AC electric fields, as detected by NMR spectroscopy. This experiment benefits simultaneously from the advantages of NMR for studying both solids and liquids. o*ngoing design and optimization of NMR hardware for these and other applications is a central activity in our research group. </P>

<TABLE cellSpacing=0 cellPadding=0 align=right border=0><TBODY><TR><TD></TD></TR></TBODY></TABLE><A name=pubList>Publications</A> "The Timescale of Loop Motion in Triosephosphate Isomerase," S. Rozovsky and A.E. McDermott, Journal of Molecular Biology, submitted (2001) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Fluorine Dipolar Measurements in Organic Solids," L. Gilchrist, K. Monde, Y. Tomita, T. Iwashita, K. Nakanishi, and A.E. McDermott, Journal of Magnetic Resonance, submitted (2001) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Dipolar Interactions in Molecules Aligned by Strong AC Electric Fields," A. Peshkovsky and A.E. McDermott, Journal of Magnetic Resonance, 147, 104*109 (2000) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Partial NMR Assignments of Uniformly (13C, 15N)-Labeled BPTI in the Solid State," A.E McDermott, T. Polenova, A. Bockmann, K.W. Zilm, and G.T. Montellione, Journal of Biomolecular NMR, 16, 209*219 (1999) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Solid State NMR Studies of Hydrogen Bonding in a Citrate Synthase Inhibitor Complex," Z. Gu, G.D. Drueckhammer, L.Kurz, K. Liu, D.P. Martin, and A.E. McDermott, Biochemistry, 38, 8022*8031 (1999) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Deuterium Magic Angle Spinning Studies of Substrates Bound to Cytochrome P450," H. Lee, P.R. Ortiz de Montellano, and A.E. McDermott, Biochemistry, 38, 10808*10813 (1999) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"A Coherent Mixing Mechanism Explains the Photoinduced Nuclear Polarization in Photosynthetic Reaction Centers," T. Polenova and A.E. McDermott, Journal of Physical Chemistry B, 103, 535*548 (1999) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Nuclear Magnetic Resonance Studies of Biopolymer Dynamics," A.G. Palmer III, J. Williams, A.E. McDermott, Invited contribution to Centennial Issue of the Journal of Physical Chemistry, 100, 13293*13310 (1996) <BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#"><BR xmlns:xmlns:cms="http://www.ais.columbia.edu/sws/xmlns/cucms#">"Photochemically Induced Nuclear Spin Polarization in Bacterial Photosynthetic Reaction Centers: Assignments of the Chemical Shifts," M. Zysmilich and A.E. McDermott, Journal of the American Chemical Society, 118, 5867*5873 (1996