NMR wisdom:Research Groups

Research Groups

• The Netherlands
• Biophysical Chemistry, University of Nijmegen
  The central research theme at the department of Biophysical Chemistry concerns the study of biomolecular interactions of proteins, RNA, DNA, and their complexes. High-resolution NMR is the predominant technique employed in the studies, although other biophysical techniques are also routinely used.
• Sattler, Michael
  Current projects focus on protein/protein and protein/RNA interactions at the pre-mRNA intron during the assembly of the pre-spliceosome.
  
  United States
• Dr. Ann McDermott, Columbia University
  Research areas: - NMR Structural Studies of Membrane Proteins - Enzymes, Hydrogen Bonding Geometry, and Dynamics - NMR Methods Development, Enhanced Signals, and Alignment
• Dr. Deborah Wuttke
  Description of Dr. Wuttke research from her faculty web page: "Our laboratory investigates interesting biological systems from structural, biophysical and biochemical perspectives. These studies further our understanding of the biology of the systems studied as well as provide insights into the fundamental nature of protein structure and function. The systems selected for study encompass several rapidly developing areas in biology and biochemistry, including telomere biology, viral replication, the estrogen receptor, and protein stability."
• Montelione, Gaetano
  The general aim of Dr. Montelione's research is to implement NMR spectroscopy as an enabling technology for structural and functional genomics. Montelione and his group develop and refine methods for protein solution structure determination, and apply these techniques to proteins of pharmaceutical or medical interest.
• Volkman, Brian
  Dr. Volkman's work focuses on the structural biology of immunological signaling molecules and the use of NMR spectroscopy in structural genomics
• Wagner, Gerhard
  Gerhard Wagner's group
  
  Canada
• Arrowsmith, Cheryl
  A citation about Cheryl Arrowsmith's research interests: "My research interests focus on the structure-function relationships of proteins involved in the control of gene expression and the cell cycle. The goals of our research are to understand at the atomic level the origins of protein-DNA recognition by transcription factors and how this process is modulated by cofactors, phosphorylation, and protein-protein interactions... We use multidimensional nuclear magnetic resonance (NMR) spectroscopy in conjunction with biochemical analysis to study the structures of proteins, protein-DNA and protein-protein complexes in solution."
• Donaldson, Logan
  Description of Prof. Donaldson's research interests from his web page: "My research focuses on understanding the how transcription factors and enzymes modify their conformation and partnerships upon receiving signals. These signals may include the binding of ligands or post-translational modifications such as phosphorylation. Nuclear magnetic resonance (NMR) spectroscopy is routinely used to determine atomic-level structures of the protein complexes studied in the laboratory. As proteins are flexible at wide range of timescales, NMR spectroscopy is also used to monitor the dynamic changes that proteins undergo upon receiving signals. "
• Forman-Kay, Julie
  Description of Forman-Kay's group research from the group web site: "We study various aspects of modular binding domains involved in signal transduction using NMR and other techniques. Ongoing projects in the lab include: - structure determination of domains and binding partners - elucidating the role of backbone and side chain dynamics in ligand binding - thermodynamic analyses of protein folding and protein - protein interactions - protein folding and stability"
• Gehring, Kalle
  Description of Kalle Gehring's group research from his web page: "Our interests are centered on the application of Nuclear Magnetic Resonance (NMR) spectroscopy to the study of protein and nucleic acid structures. Recent structures include peptide mimetics of Nerve Growth Factor, and a peptide binding domain (PDZ domain) involved in signal transduction. Currently, we are studying several new systems including a protein homeodomain that forms a ternary complex with DNA and a peptide co-factor and a nucleotide exchange factor involved in protein translation. Our laboratory combines techniques from chemistry, molecular biology and bio-informatics in the quest for a deeper understanding of molecular recognition in biological systems."
• Goto, Natalie
  Description of Natalie Goto\'s research from her web site: "My research laboratory focuses on the application and development of solution NMR methods to address some of the problems associated with structure determination of membrane proteins."
• Ikura, Mitsu
  Description of Prof. Ikura's research interests from his web page: " Our laboratory is interested in finding out how the molecular network governing signal transduction processes works in living systems and what exactly happens, at an atomic/molecular level, when some of signalling molecules are mutated or damaged. For this goal, we investigate structure-function relationships of signalling proteins by means of biochemical and biophysical methods such as nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, and fluorescence resonance energy transfer (FRET) imaging microscopy. These methods enable us to determine the three-dimensional atomic structures of proteins and protein complexes (NMR, X-ray) as well as their dynamic behaviors in living cells (FRET). "
• Kay, Lewis
  Lewis Kay's description of his group research from his web site: "We study nuclear magnetic resonance spectroscopy and its application to biomolecules. Our work centres around the development of new techniqes to study study the motions of proteins in solution. Also, we develop techniques to study extremely large proteins. "
• McIntosh, Lawrence
  Description of Prof. McIntosh's research interests from his web page: "My research focusses on the structure and dynamics of proteins and protein-DNA complexes. Using a combination of multi-dimensional NMR spectroscopy, physical biochemistry, and molecular biology, my aim is to explore the connections between the structure and function of proteins."
• Meiering, Elizabeth Research Interests (from the group web site): "Proteins: structure, dynamics, folding, and function. High resolution nuclear magnetic resonance spectroscopy. Optical spectroscopies. Biocomputing and Protein Engineering. Proteins currently under invesigation include: hisactophilin (b-trefoil protein); dihydrofolate reductase; ribonuclease H from Escherichia coli and HIV-I; human superoxide dismutase."
• Melacini, Giuseppe
  Areas of research (from Dr. Melacini's website): [1] The mechanism of nucleation and of inhibition of amyloid fibrils: Amyloid depositions are linked to several pathologies, including Alzheimer’s, Parkinson’s, Type II diabetes and mad-cow (BSE) diseases. We plan to use NMR to understand how amyloid deposits can be detected and prevented. [2] Protein hydration dynamics: Protein-water interactions are one of the essential driving forces of protein folding. [3] Development of NMR methods for high-throughput structural genomics. [4] We are also involved in several collaborative efforts to understand how ligand-induced allosteric conformational changes of signaling proteins are related to their dynamics.
• Shaw, Gary
  Description of projects in Gary Shaw lab from Dr. Shaw web page: "Calcium-binding Proteins Project Projects focus on the three-dimensional structures of calcium-binding proteins and their roles in health and disease. We use physical biochemical techniques such as high resolution NMR spectroscopy, analytical centrifugation, fluorescence and circular dichroism to probe structure/function relationships... Ubiquitin Pathway Protein Interactions... ...We are using NMR spectroscopy to determine interactions between ubiquitin and the E1, E2 and E3 proteins. "
• Smith, Steven
  Description of lab research from Steven Smith\'s web page: "Our lab is currently interested in proteins of three biological systems or processes: - the structural aspects behind the assembly of the cellulose-degrading complex in thermophile bacteria; - apo(a) kringle assembly and interactions; - calcium activation of the Ca2+-dependent thiol protease calpain. "
• Spyracopoulos, Leo
  Description of Dr. Spyracopoulos's research interests from his web page: "The research focus of my laboratory is to gain an understanding of biological functions carried out by proteins by determination of the structures of proteins and their complexes, and the kinetics, dynamics, and thermodynamics of proteins and protein-ligand interactions. Application of nuclear magnetic resonance (NMR) spectroscopic techniques allow me to attain my overall research goals. My objective is to gain an understanding of the mechanism of protein ubiquitination at the molecular level by studying the structure, interactions, and dynamics of the human UEV–Ubc13 protein heterodimers."
• Sykes, Brian
  Description of group research from its web page: "Our research involves the elucidation of the structure, dynamics and function of proteins. In particular, we are interested in the function of the proteins that make up the thin filament of skeletal and cardiac muscle and regulate contraction; focusing on the calcium sensitive interactions between actin, tropomyosin, and troponin and the conformational changes that occur in these proteins upon binding calcium ions. Our major tool in this regard is nuclear magnetic resonance spectroscopy, especially the use of multi-nuclear and multi-dimensional NMR techniques combined with the computational techniques of energy minimization and molecular dynamics to determine the structure of proteins in solution. We are also studying the structure of several growth factors such as TGF-alpha, and the interaction of those growth factors with their receptors, as well as exchangeable apolipoproteins and antifreeze proteins. "
• Vogel, Hans
  Description of group research from Hans Vogel\'s web site: "The three main research projects right now are calcium-binding regulatory proteins, structure-function analysis of antimicrobial peptides as well as studies of iron uptake processes in bacteria. Inspection of the list of publications will give you an idea about the scope of the research work. In all cases we use structural techniques (mostly NMR spectroscopy) and other biophysical approaches (eg microcalorimetry, fluorescence spectroscopy) to characterize the interactions between proteins and peptides with one another, or with metal ions or membranes. "
• Wishart, David
  Description of group research from David Wishart's web site: "Our laboratory is currently working in three areas of pharmaceutical biotechnology research: - Protein-Based Drug Targeting and Medical Diagnostics: the development of new methods for the targeted delivery of drugs or diagnostic agents using peptide or protein-based vehicles; - NMR Technology Development: the development novel applications in NMR spectroscopy to facilitate structure-aided drug design; - Pharmaceutical Bioinformatics: the development of innovative bioinformatics and modeling software for improved protein/peptide analysis. "
  
  Directories
• List of Canadian NMR/MRI scientists on NANUC web site