A5075658290- Advanced NMR Techniques and Applications
- Protein Structure and Dynamics
- Lipid Membrane Structure and Behavior
- RNA and protein synthesis mechanisms
- Enzyme Structure and Function
- Solid-state spectroscopy and crystallography
- Electron Spin Resonance Studies
- NMR spectroscopy and applications
- Bacteriophages and microbial interactions
- DNA and Nucleic Acid Chemistry
- Influenza Virus Research Studies
- Bacterial Genetics and Biotechnology
- Advanced MRI Techniques and Applications
- Ion channel regulation and function
- Tuberculosis Research and Epidemiology
- Atomic and Subatomic Physics Research
- Spectroscopy and Quantum Chemical Studies
- Molecular spectroscopy and chirality
- Photoreceptor and optogenetics research
- Muon and positron interactions and applications
- Mass Spectrometry Techniques and Applications
- Nanopore and Nanochannel Transport Studies
- Antimicrobial Peptides and Activities
- Supramolecular Self-Assembly in Materials
- Force Microscopy Techniques and Applications
Florida State University
2016-2025
National High Magnetic Field Laboratory
2015-2025
Institute of Molecular Biology and Biophysics
2014-2025
Royal Liverpool University Hospital
2022
University of Liverpool
2022
American Meteorological Society
2007
University of Louisville
2006
Vanderbilt University
2006
National Institute of Chemical Physics and Biophysics
2002
Centre National de la Recherche Scientifique
2002
Solid-state nuclear magnetic resonance spectroscopy of uniformly aligned preparations gramicidin A in lipid bilayers has been used to elucidate a high-resolution dimeric structure the cation channel conformation solely on basis amino acid sequence and 144 orientational constraints. This initial defines helical pitch as single-stranded, fixes number residues per turn at six seven, specifies helix sense right-handed, identifies hydrogen bonds. Refinement this yields reasonable hydrogen-bonding...
The M2 protein from the influenza A virus, an acid-activated proton-selective channel, has been subject of numerous conductance, structural, and computational studies. However, little is known at atomic level about heart functional mechanism for this tetrameric protein, a His(37)-Trp(41) cluster. We report structure conductance domain (residues 22 to 62) in lipid bilayer, which displays defining features native that have not attainable structures solubilized by detergents. propose cluster...
The heart of the H+ conductance mechanism in homotetrameric M2 channel from influenza A is a set four histidine side chains. Here, we show that protonation third these imidazoles coincides with acid activation this transmembrane and that, at physiological pH, closed by two imidazole-imidazolium dimers, each sharing low-barrier hydrogen bond. This unique construct succeeds distributing pair charges over rings many atoms low dielectric environment to minimize charge repulsion. These dimers...
Abstract The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in liquid crystalline bilayer environment. exposure hydrophilic backbone structure is minimized through hydrogen bond geometry imposed by low dielectric lipid high‐resolution monomer detailed description its orientation with respect to were achieved using orientational restraints solid‐state NMR. With this unique information, tetrameric H + channel constrained substantially....
An interhelical distance has been precisely measured by REDOR solid-state NMR spectroscopy in the transmembrane tetrameric bundle of M2-TMP, from M2 proton channel influenza A viral coat. The high-resolution structure helical backbone determined using orientational restraints uniformly aligned peptide preparations hydrated dimyristoylphosphatidylcholine bilayers. Here, between (15)N(pi) labeled His37 and (13)C(gamma) Trp41 is to be less than 3.9 A. Such a short distance, combination with...
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...
Orientational constraints generated from solid-state NMR of uniformly aligned gramicidin A in hydrated lipid bilayers have been used to determine the indole ring orientations for four tryptophans monomer with respect bilayer normal and channel axis. 15N epsilon 1 labeled tryptophan has incorporated into at positions 9, 11, 13, 15. The chemical shift tensor orientation oriented N-H bond via doubly sample which 1-1H exchanged 2H. By observation dipolar coupled powder pattern amino acid, sigma...
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.
Abstract Amphipathic helices in membrane proteins that interact with the hydrophobic/hydrophilic interface of lipid bilayer have been difficult to structurally characterize. Here, backbone structure and orientation an amphipathic helix full‐length M2 protein from influenza A virus has characterized. The studied hydrated DMPC/DMPG bilayers above gel liquid‐crystalline phase transition temperature by solid‐state NMR spectroscopy. Characteristic PISA (Polar Index Slant Angle) wheels reflecting...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTGramicidin cation channel: an experimental determination of the right-handed helix sense and verification .beta.-type hydrogen bondingL. K. Nicholson T. A. CrossCite this: Biochemistry 1989, 28, 24, 9379–9385Publication Date (Print):November 1, 1989Publication History Published online1 May 2002Published inissue 1 November 1989https://pubs.acs.org/doi/10.1021/bi00450a019https://doi.org/10.1021/bi00450a019research-articleACS PublicationsRequest reuse...
The M2 protein of influenza virus A is a proton-selective ion channel activated by pH. Structure determination solid-state and solution NMR X-ray crystallography has contributed significantly to our understanding, but activation may involve conformations not captured these studies. Indeed, data demonstrate that the possesses significant conformational heterogeneity. Here, we report molecular dynamics (MD) simulations transmembrane domain (TMD) in absence presence antiviral drug amantadine....