A5046677875- Advanced NMR Techniques and Applications
- Protein Structure and Dynamics
- NMR spectroscopy and applications
- Lipid Membrane Structure and Behavior
- Solid-state spectroscopy and crystallography
- Electron Spin Resonance Studies
- Advanced MRI Techniques and Applications
- Bacteriophages and microbial interactions
- RNA and protein synthesis mechanisms
- Molecular spectroscopy and chirality
- Enzyme Structure and Function
- DNA and Nucleic Acid Chemistry
- Muon and positron interactions and applications
- Antimicrobial Peptides and Activities
- Glycosylation and Glycoproteins Research
- Chemical Synthesis and Analysis
- HIV Research and Treatment
- Hepatitis C virus research
- Hemoglobin structure and function
- Mass Spectrometry Techniques and Applications
- Monoclonal and Polyclonal Antibodies Research
- Trace Elements in Health
- Supramolecular Self-Assembly in Materials
- Crystallography and Radiation Phenomena
- Analytical Chemistry and Chromatography
University of California, San Diego
2015-2024
North Carolina State University
2010
University of South Carolina
2009
University of Arkansas at Fayetteville
2008
University of Pennsylvania
1996-2007
University of Houston
2005
University of Connecticut
2005
Sanford Burnham Prebys Medical Discovery Institute
2002-2004
University of Minnesota
2002-2003
Biotechnology Institute
2003
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSelection of nonprotonated carbon resonances in solid-state nuclear magnetic resonanceS. J. Opella and M. H. FreyCite this: Am. Chem. Soc. 1979, 101, 19, 5854–5856Publication Date (Print):September 1, 1979Publication History Published online1 May 2002Published inissue 1 September 1979https://pubs.acs.org/doi/10.1021/ja00513a079https://doi.org/10.1021/ja00513a079research-articleACS PublicationsRequest reuse permissionsArticle...
Abstract Magainin 2 is a 23‐residue peptide that forms an amphipathic α ‐helix in membrane environments. It functions as antibiotic and known to disrupt the electrochemical gradients across cell membranes of many bacteria, fungi, some tumor cells, although it does not lyse red blood cells. One‐ two‐dimensional solid‐state 15 N NMR spectra specifically N‐labeled magainin oriented bilayer samples show secondary structure essentially entire ‐helix, immobilized by its interactions with...
The dipolar coupling between 14N and 13C is not suppressed by magic angle sample spinning because the relatively large quadrupole interaction shifts axis of quantization spins away from direction applied field. resulting resonance line shapes are influenced sign, magnitude, asymmetry parameter tensor; internuclear distance; magnitude magnetic field; orientation vector in principal system electric field gradient. It demonstrated that one or more these parameters can be determined NMR data if...
Complete resolution of the amide resonances in a three-dimensional solid-state NMR correlation spectrum uniformly 15 N-labeled membrane protein oriented phospholipid bilayers is demonstrated. The three orientationally dependent frequencies, 1 H chemical shift, H– N dipolar coupling, and associated with each resonance are responsible for among provide sufficient angular restrictions structure determination. Because completely immobilized by phospholipids on relevant time scales (10 kHz),...
Bacteria carrying plasmids with the mer operon, which encodes proteins responsible for bacterial mercury detoxification system, have ability to transport Hg(II) across cell membrane into cytoplasm where it is reduced Hg(0). This significant because metallic relatively nontoxic and volatile thus can be passively eliminated. The structures of mercury-bound forms merP, periplasmic protein, binds transfers protein merT, been determined in aqueous solution by multidimensional NMR spectroscopy....
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDetection of individual carbon resonances in solid proteinsS. J. Opella, M. H. Frey, and T. A. CrossCite this: Am. Chem. Soc. 1979, 101, 19, 5856–5857Publication Date (Print):September 1, 1979Publication History Published online1 May 2002Published inissue 1 September 1979https://pubs.acs.org/doi/10.1021/ja00513a080https://doi.org/10.1021/ja00513a080research-articleACS PublicationsRequest reuse permissionsArticle Views179Altmetric-Citations180LEARN...
The extremely chemically resistant component of the cell wall spores, pollens, and some microorganisms, sporopollenin, is generally accepted to be derived from carotenoids or carotenoid esters. However, we report here that 13C NMR analyses sporopollenin several sources shows this widely held view incorrect, with one possible exception. Sporopollenin not a unique substance but rather series related biopolymers largely saturated precursors such as fatty acids. contain varying amounts oxygen in...
Solid-state NMR spectroscopy is emerging as a new approach in the structural investigations of peptides and proteins membrane bilayers. Orientational parameters obtained from samples aligned on glass plates have been used to determine their secondary structures orientations bilayer. They also determination high resolution structure gramicidin. Additional information, distance measurements between pairs different nuclei like has bilayers using magic angle spinning methods.
The two-dimensional NMR procedure of separated local field spectroscopy [J. S. Waugh, Proc. Natl. Acad. Sci. USA 73, 1394 (1976)] is applied to fibers highly oriented polyethylene. 1H decoupled 13C chemical shift spectrum the fiber parallel external magnetic a single line, while distinctive powder pattern results from perpendicular orientation that in excellent agreement with calculations. 13C–1H dipolar splitting 45 kHz at σ33 and nonexistent σ22 consistent perfectly aligned methylene...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInfluence of nitrogen-14 on carbon-13 NMR spectra solidsJ. G. Hexem, M. H. Frey, and S. J. OpellaCite this: Am. Chem. Soc. 1981, 103, 1, 224–226Publication Date (Print):January 1981Publication History Published online1 May 2002Published inissue 1 January 1981https://pubs.acs.org/doi/10.1021/ja00391a057https://doi.org/10.1021/ja00391a057research-articleACS PublicationsRequest reuse permissionsArticle Views361Altmetric-Citations143LEARN ABOUT THESE...
Viroporins constitute a class of viral membrane proteins with diverse roles in the life cycle. They can self-assemble and form pores within bilayer that transport substrates, such as ions genetic material, are critical to infection However, there is little known about oligomeric state most viroporins. Here, we use native mass spectrometry detergent micelles uncover patterns oligomerization full-length SARS-CoV-2 envelope (E) protein, poliovirus VP4, HIV Vpu. Our data suggest E protein...
A solid-state NMR approach for simultaneous resonance assignment and three-dimensional structure determination of a membrane protein in lipid bilayers is described. The based on the scattering, hence descriptor "shotgun," (15)N-labeled amino acids throughout sequence (and resulting spectra). samples are obtained by expression bacteria grown media which one type acid labeled others not. Shotgun short-circuits laborious time-consuming process obtaining complete sequential assignments prior to...
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from membrane environment of cell, where spans phospholipid bilayer, to newly extruded virus particles. Nuclear magnetic resonance (NMR) studies show membrane-bound form 46-residue Pf1 be surprisingly complex with five distinct regions. The secondary structure consists long hydrophobic helix (residues 19 42) that bilayer and short amphipathic 6 13)...