Biomolecular Structure and Dynamics

 
 

Faculty

Stephen Sprang, Center Director

Our laboratory is interested in the structural biology of cellular signaling through heterotrimeric G proteins.  We use the tools of X-ray crystallography, enzymology and molecular biology to explore and understand the structural and chemical mechanisms  by which G proteins regulate cellular processes and are themselves regulated.
http://dbs.umt.edu/people/faculty/facultydetail.aspx?id=941

Bruce Bowler, Chair, BSD Graduate Program

My laboratory is engaged in research on protein folding and biological electron transfer. Our focus in protein folding is on the properties of denatured proteins and how these properties affect the early events in the folding process. Our work on electron transfer emphasizes how protein dynamics modulates electron transfer rates.
http://www.umt.edu/chemistry/BruceBowler.htm

For more information on the graduate program: http://www.cas.umt.edu/biomolecular/contact.htm

Rich Bridges

Bridges' group focuses on the structure, biochemical mechanism and pharmacology of  integral membrane glutamate transporter proteins, as well as the functional role these systems play in the central nervous system.
http://www.health.umt.edu/schools/biomed/faculty/bridges.htm

Klára Briknarová

Professor Briknarová is interested in protein structure and function.
http://www.umt.edu/chemistry/faculty/briknarova.htm

Xi Chu

Our research is directed towards understanding the electronic structure, geometry, and dynamics of molecules of technological or fundamental interests. Ab initio or semi-empirical quantum mechanics and numerical approaches are developed to obtain desired results

http://www.umt.edu/chemistry/faculty/chu.htm

Dianne DeCamp

Our lab is interested in studying the structure and function of integral membrane proteins, which typically reside and function in a cell’s plasma membrane. Transmembrane proteins, including receptors, are capable of transducing responses from the outside of the cell to the interior through ligand binding and structural rearrangement.  They are involved in many aspects of cell homeostasis, including signal transduction, ion and pH regulation and cellular communications, as well as cancer and disease states. Biochemical techniques and X-ray crystallography are used to elucidate ligand binding and the interactions between membrane proteins in complexes. We use eukaryotic and bacterial heterologous expression systems in order to obtain sufficient quantities of proteins for study, and maintain a core facility for insect cell expression. Current projects involve the study of the β2 adrenergic receptor in complex with the G protein heterotrimer,  the complex of Junin virus glycoprotein 2 and SSP, and Excitatory Amino Acid Transporter 3 (EAAT3).

http://www.health.umt.edu/schools/biomed/faculty/decamp.htm

John Gerdes

Gerdes reasearch efforts are focussed on investigating structure and function aspects of select transport proteins found within the central nervous system (CNS), effected by construction and analysis of contemporary protein computational models, the design and testing of small molecules (ligands) that intereact with the transporters, and evaluating the transporters in vivo with positron emission tomography functional imaging studies.
http://www.health.umt.edu/schools/biomed/faculty/gerdes.htm

Mark Grimes

Nerve growth factor signal transduction occurs in some surprising intracellular locations.  The receptors continue to signal for a long time after internalization and activate unique signalling pathways.
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=884

Jesse Hay

Mammalian Cell Biology, Intracellular Membrane Trafficking
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=886

Walt Hill

We are determining the time-dependent gymnastics of the ribosome as it performs its duty to translate the genetic message into proteins.
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=923

Darrell Jackson

Our studies have significant implications for linking dysfunctions in G-protein-coupled receptor (GPCR) signaling with numerous neurological disorders that includes Alzheimer's disease, Parkinson's disease, and stroke. A major focus in the laboratory is identifying and characterizing the mechanisms that regulate the endosomal sorting of internalized cell surface GPCRs in neurons. Sequestration of cell surface neurotransmitter receptors, such as GPCRs, is one mechanism utilized by neurons to terminate receptor signaling. The mechanism regulating endosomal sorting of internalized GPCRs in neurons remains unclear. A second focus in the laboratory involves elucidating the underlying mechanisms that mediate the polarize sorting of selective GPCRs in neurons to either dendritic or axonal compartments.
http://www.health.umt.edu/schools/biomed/faculty/jackson.htm

Michael Kavanaugh

Research in the Kavanaugh laboratory focuses on neurotransmitter transporters and ion channels, membrane proteins involved in reuptake and signaling in neurons using techniques including voltage-clamp recording, radiotracer flux measurement, and fluorescent labeling.
http://www.health.umt.edu/schools/biomed/faculty/kavanaugh.htm

Bill Laws

We use fluorescence spectroscopy and other physical methods to examine the role of structure and dynamic motion on the function of biological macromolecules and their interactions; investigate the X and Y positional dependence of different amino acids in collagen’s [-Gly-X-Y-]n repeating trimer sequence; study the role of protein and DNA dynamics during the enzymatic repair of DNA damage; evaluate the effects of conformational changes and local dynamic motions in the proteins initiating blood coagulation.
http://www.umt.edu/chemistry/faculty/laws.htm

Stephen Lodmell

We are investigating how the structure of HIV RNA regulates viral replicative processes including translation of viral proteins, encapsidation, splicing, and RNA dimerization.
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=892

Michele McGuirl

My laboratory is devoted to the study of metalloproteins; ongoing research projects range from understanding metal ion homeostasis to studying the structure and function of metalloproteins.
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=897

Nicholas Natale

The Natale lab is interested in the role of chirality and conformational dynamics in bioactive small molecules. Specifically, the group has developed synthetic methodology which is applicable to the development of Structure Activity Relationships (SAR) for a number of isoxazole containing drug candidates.
http://www.health.umt.edu/schools/biomed/faculty/natale.htm

Jack Nunberg

We study the biogenesis, structure and function of viral envelope glycoproteins.
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=900

Keith Parker

Research in the Parker laboratory centers on the molecular pharmacology of serotonin receptors, especially those which may be involved in nervous system disorders such as migraine headache, anxiety, and panic. Recent work has utilized synthetic peptide probes of the interface between the human 5HT1a receptor and the G protein coupled signal transduction system. Cloned receptors and G proteins are obtained from serially cultured cell lines. Structure-activity studies based upon a parent intracellular loop 3 peptide have utilized both binding and functional second messenger formats. Ultimately, the probes will be useful in multidimensional NMR studies in which the peptide-G protein surface will serve as a model of the native receptor-G protein coupling and activation sequence. The 5HT1a receptor is a member of the large family of seven transmembrane domain, G protein coupled neurotransmitter and hormone receptors. Understanding of the structural characteristics of these receptors is converging from a variety of experimental approaches. Work in the Parker laboratory in conjunction with collaborators provides information which will aid in identifying similarities and differences between individual receptors in this biologically conserved group of signaling molecules. Although this work is conducted at the basic pharmacology level, new drugs may be developed since the receptor/G protein interface is a potential pharmacological target.
http://www.health.umt.edu/schools/biomed/faculty/parker.htm  

Nigel Priestley

The Priestley group uses a combination of genetic engineering and chemical synthesis to study the macromolecular complexes responsible for the catalysis of polyketide biosynthesis with the aim of reprogramming the natural systems to provide new anti-infective and anti-cancer drugs.
http://www.umt.edu/chemistry/faculty/priestley.htm

Ed Rosenberg

We are developing site selective biomarkers based on Organometallic metal clusters containing pseudo nucleobases.  To date we have observed remarkable site selectivity and the ability to infuse the marker into biomacrolmolecular single crystal assemblies.
http://www.umt.edu/chemistry/faculty/rosenberg.htm

Sandy Ross

The Ross group uses biological fluorescence spectroscopy to investigate protein-protein and protein membrane interactions in initiation of blood coagulation and protein-protein and protein-nucleic acid interactions in regulation of transcription and repair of damaged DNA.
http://www.umt.edu/chemistry/faculty/ross.htm

Scott Samuels

Our goal is to dissect the role of DNA structure, DNA topoisomerases, architectural DNA-binding proteins, alternate sigma factors, and other transcription factors in the regulation of gene expression and the replication of linear DNA in bacteria.
http://dbs.umt.edu/people/faculty/facultyDetail.aspx?id=905

Chuck Thompson

Research in our group seeks to better understand the small molecule-protein interactions in the glutamatergic and cholinergic neurotransmitter systems using chemical, biological and proteomic approaches.
http://www.health.umt.edu/schools/biomed/faculty/thompson.htm

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