A5070315385- Mass Spectrometry Techniques and Applications
- Enzyme Structure and Function
- Photosynthetic Processes and Mechanisms
- RNA and protein synthesis mechanisms
- Protein Structure and Dynamics
- Photoreceptor and optogenetics research
- Algal biology and biofuel production
- Ion channel regulation and function
- Bacterial Genetics and Biotechnology
- Advanced Proteomics Techniques and Applications
- Bacteriophages and microbial interactions
- Receptor Mechanisms and Signaling
- Ion-surface interactions and analysis
- Antioxidant Activity and Oxidative Stress
- Microfluidic and Capillary Electrophoresis Applications
- Electrochemical Analysis and Applications
- X-ray Spectroscopy and Fluorescence Analysis
- Microbial Fuel Cells and Bioremediation
- Molecular Biology Techniques and Applications
- Nicotinic Acetylcholine Receptors Study
- Monoclonal and Polyclonal Antibodies Research
- Metabolomics and Mass Spectrometry Studies
- Alzheimer's disease research and treatments
- RNA modifications and cancer
- Metalloenzymes and iron-sulfur proteins
Lawrence Berkeley National Laboratory
2015-2024
Vellore Institute of Technology University
2023
Michigan State University
2018
Elucid Bioimaging
2018
Case Western Reserve University
2007-2015
Tata Institute of Fundamental Research
2000-2008
Brookhaven National Laboratory
2007
Albert Einstein College of Medicine
2004-2007
European Molecular Biology Laboratory
2001
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus enters host cells via an interaction between its Spike protein and the cell receptor angiotensin-converting enzyme (ACE2). By screening a yeast surface-displayed library of synthetic nanobody sequences, we developed nanobodies that disrupt ACE2. Cryo-electron microscopy (cryo-EM) revealed one nanobody, Nb6, binds in fully inactive conformation with binding domains locked into their inaccessible down state, incapable...
Protection from too much light Photosynthetic organisms protect themselves using pigment photoswitches that absorb excess energy. Leverenz et al. analyzed the structure of an active, energy-dissipating form orange carotenoid protein (OCP) a cyanobacterium. When activated by light, OCP moves its hydrophobic 12 Å within to accommodate nonphotochemical quenching broader photosynthetic antenna complex. Science , this issue p. 1463
Structural water molecules may act as prosthetic groups indispensable for proper protein function. In the case of allosteric activation G protein-coupled receptors (GPCRs), likely imparts structural plasticity required agonist-induced signal transmission. Inspection structures GPCR superfamily members reveals presence conserved embedded important to Coupling radiolytic hydroxyl radical labeling with rapid H(2)O(18) solvent mixing, we observed no exchange these waters bulk in either ground...
Significance The orange carotenoid protein (OCP) is critical for the antenna-associated energy-dissipation mechanism of cyanobacteria under high light conditions. We show that activation causes a global conformation change, complete separation two domains OCP. Such conformational change has been postulated to be prerequisite interaction with antenna. also identify local structural changes in residue solvent accessibility and roles water molecules By combining small-angle scattering,...
Bacterial microcompartments (BMCs) encapsulate enzymes within a selectively permeable, proteinaceous shell. Carboxysomes are BMCs containing ribulose-1,5-bisphosphate carboxylase oxygenase and carbonic anhydrase that enhance carbon dioxide fixation. The carboxysome shell consists of three structurally characterized protein types, each named after the oligomer they form: BMC-H (hexamer), BMC-P (pentamer), BMC-T (trimer). These types form cyclic homooligomers with pores at center symmetry...
Structural mapping of proteins and nucleic acids with high resolution in solution is critical importance for understanding their biological function. A wide range footprinting technologies have been developed over the last ten years to address this need. Beamline X28C, a white-beam X-ray source at National Synchrotron Light Source Brookhaven Laboratory, functions as platform synchrotron research further technology development growing field. An expanding set user groups utilize national...
Abstract Human estrogen receptor alpha (hERα) is a hormone-responsive nuclear (NR) involved in cell growth and survival that contains both DNA-binding domain (DBD) ligand-binding (LBD). Functionally relevant inter-domain interactions between the DBD LBD have been observed several other NRs, but for hERα, detailed structural architecture of complex unknown. By utilizing integrated complementary techniques small-angle X-ray scattering, hydroxyl radical protein footprinting computational...
ABSTRACT Without an effective prophylactic solution, infections from SARS-CoV-2 continue to rise worldwide with devastating health and economic costs. gains entry into host cells via interaction between its Spike protein the cell receptor angiotensin converting enzyme 2 (ACE2). Disruption of this confers potent neutralization viral entry, providing avenue for vaccine design therapeutic antibodies. Here, we develop single-domain antibodies (nanobodies) that potently disrupt ACE2. By screening...
X-ray footprinting (XF) is an important structural biology tool used to determine macromolecular conformations and dynamics of both nucleic acids proteins in solution on a wide range timescales. With the impending shut-down National Synchrotron Light Source, it ever more that this continues be developed at other synchrotron facilities accommodate XF users. Toward end, collaborative program has been initiated Advanced Source using white-light bending-magnet beamlines 5.3.1 3.2.1....
Achieving fast electron transfer between a material and protein is long-standing challenge confronting applications in bioelectronics, bioelectrocatalysis, optobioelectronics. Interestingly, naturally occurring extracellular proteins bind to reduce metal oxides enough enable cell growth, thus could offer insight into solving this coupling problem. While structures of several are known, an understanding how these their oxide substrates has remained elusive because abiotic–biotic interface...
Bacterial microcompartments (BMCs) are protein-bound organelles found in some bacteria that encapsulate enzymes for enhanced catalytic activity. These compartments spatially sequester within semipermeable shell proteins, analogous to many membrane-bound organelles. The proteins assemble into multimeric tiles; hexamers, trimers, and pentamers, these tiles self-assemble larger assemblies with icosahedral symmetry. While shells the predominant form
Water is critical for the structure, stability, and functions of macromolecules. Diffraction NMR studies have revealed structure dynamics bound waters at atomic resolution. However, localizing sites measuring waters, particularly on timescales relevant to catalysis macromolecular assembly, quite challenging. Here we demonstrate two techniques: first, temperature-dependent radiolytic hydroxyl radical labeling with a mass spectrometry (MS)-based readout identify bulk water interactions surface...
Hybrid structural methods have been used in recent years to understand protein-protein or protein-ligand interactions where high resolution crystallography NMR data on the protein of interest has limited. For G protein-coupled receptors (GPCRs), structures native forms other than rhodopsin not yet achieved; gaps our knowledge filled by creative studies that developed stable multiple means. The neurotransmitter serotonin (5-hydroxytryptamine) is a key GPCR-based signaling molecule affecting...