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  STRUCTURAL BIOLOGY  
 

• Rebecca DuBois (BME) Structure, Function, and Engineering of Virus Proteins
• Ted Holman (Chem) Lipoxygenase Inhibitors as Potential Anti-Inflammatory Drugs
• Melissa Jurica (MCD) Structure and Functional Analysis of Spliceosomes
• Kevin Karplus (BME) Protein Structure Prediction and Design
• Glenn Millhauser (Chem) Remarkable Protein Structures ..... and Where They Go Wrong
• Harry Noller (MCD) Structure and Function of the Ribosome
• Carrie Partch (Chem) Exploring the Molecular Basis for Circadian Timekeeping in Mammals
• Seth Rubin (Chem) Molecular Mechanisms of Cell Cycle Regulation and Cancer
• Bill Scott (Chem) Understanding the Structure-based Mechanisms of Ribozyme-based Theraputic Agents
• Nik Sgourakis (Chem) Modelling the Structures of Protein Complexes from Sparse Experimental Data
• Michael Stone (Chem) Structure, Function, and Assembly of the Telomerase Ribonucleoprotein

Prof DuBoisStructure, Function, and Engineering of Virus Proteins

Rebecca DuBois, Biomolecular Engineering

Professor DuBois is a structural biologist studying viral surface and replication proteins. She uses her discoveries to design novel vaccines, to develop nanoscale drug delivery vehicles, and to develop antiviral therapeutics. [More]

DuBois Publications Rebecca Dubois' E-Mail

 


Prof HolmanLipoxygenase Inhibitors as Potential Anti-Inflammatory Drugs

Ted Holman, Dept. of Chemistry & Biochemistry

Lipoxygenases are enzymes implicated in a broad range of inflammatory diseases, such as diabetes, heart disease, and stroke, to name a few. Ted Holman's laboratory examines the enzymatic mechanism and biological function of lipoxygenase in the hopes of understanding how the enzyme functions and developing novel inhibitors. In collaboration with medical school collaborators, his laboratory has identified potent lipoxygenase inhibitors and are currently characterizing their structure/function reactivity. The results of this work will shed light on their potential as anti-inflammatory agents. [More]

Holman's Publications Ted Holman's E-Mail

Prof Melissa JuricaStructure and Functional Analysis of Spliceosomes

Melissa Jurica, MCD Biology

The Jurica lab investigates the cellular machinery responsible for editing the information contained in the RNA transcripts of nearly all of human genes. This machinery, called the spliceosome, uses a molecular “splicing” reaction to cut out intron sequences that interrupt gene transcripts and joins exon sequences to make messenger RNAs that correctly encode for proteins. Splicing is a key step of gene expression and its misregulation is linked to many genetic diseases, including cancers and neurodegenerative disease. Juric'a goal is to determine how the spliceosome is assembled and how it catalyzes the splicing reaction. The lab's reasearch will provide a basic foundation for understanding what goes wrong with splicing in disease situations. [More]

Melissa Jurica's Publications Melissa Jurica's E-Mail

Prof Kevin KarplusProtein Structure Prediction and Design

Kevin Karplus, Dept. of Biomolecular Engineering

Kevin Karplus' research group develops tools and techniques for protein structure prediction and protein design. He collaborates with Richard Hughey's group on the development of the SAM tool suite for profile hidden Markov models, particularly on developing protocols for using the tools for high-accuracy detection of remote relationships between proteins. Karplus' group has used these tools themselves to earn an international reputation for accurate prediction of protein structure: secondary structure, tertiary structure, and contact prediction. In the biannual Critical Assessment of Structure Prediction "contests", his group has presented papers (the "prize" for the contest) in CASP2 through CASP7. The group also collaborates extensively with UCSC wet-lab biologists in predicting structure and function for proteins of interest to them, and is starting work on designing novel proteins. [More]

Karplus Publications Kevin Karplus's E-Mail

Prof MillhauserRemarkable Protein Structures ..... and Where They Go Wrong

Glenn Millhauser, Department of Chemistry

In the laboratory of Glenn Millhauser, investigators use peptide synthesis and magnetic resonance to investigate the structure and function of biomolecules. These studies include analysis of proteins involved in devastating metabolic and neurological diseases. [More]

Millhauser Publications Glenn Millhauser's E-Mail

Prof Harry NOller

Structure and Function of the Ribosome

Harry Noller, MCD Biology

The Noller laboratory studies ribosome structure and function using a wide range of approaches, including X-ray crystallography, chemical probing methods, molecular genetics, comparative sequence analysis, fluorescence resonance energy transfer (FRET), including the use of single-molecule methods. The ultimate goal of these studies is to understand how the ribosome works at the molecular level: what are the moving parts of the machine, and how do they move in three dimensions to enable translation? [More]
Noller Publications Harry Noller's E-Mail

Prof Rubin Exploring the Molecular Basis for Circadian Timekeeping in Mammals

Carrie Partch , Chemistry and Biochemistry

Mammalian physiology is synchronized into 24-hour rhythms that coincide with the solar day by an intrinsic molecular clock. As a global regulator of homeostasis, disruption of the circadian clock has profound consequences on human health, leading to depression, metabolic syndromes, cancer, and premature aging. The Partch lab studies how the 24-hour periodicity of this molecular clock is generated and how it integrates with the cell cycle to limit proliferation using cell biology, biochemistry and biophysical techniques. They are also interested in chemical biology approaches to modulate clock timing with structurally informed in vitro and cell-based screening platforms. [More]

Partch Publications Carrie Partch's E-Mail


Prof RubinMolecular Mechanisms of Cell Cycle Regulation and Cancer

Seth Rubin, Chemistry and Biochemistry

The Rubin laboratory uses a variety of structural and biochemical techniques to investigate the molecular mechanisms that control the eukaryotic cell cycle. The aim is to elucidate detailed molecular pictures of protein-protein interactions and how these interactions are regulated by structural and chemical modifications. Improper regulation of these protein interaction networks is commonly associated with aberrant cell proliferation and cancer. [More]

Rubin Publications Seth Rubin's E-Mail


Prof Scott
RNA Catalysis

William Scott, Dept. of Chemistry and Biochemistry

Ribozmes are RNA-based enzymes whose comparatively recent discovery came as major surprize to the scientific community, as it has always been assumed that only proteins could be enzymes. Researchers in the Scott laboratory are trying to understand how ribozymes work, using X-ray crystallography and other biochemical and biophysical techniques. The potential use of ribozymes as therapeutic agents that target RNA viruses (such as HIV) and pathological mRNAs (such as oncogene transcripts) is well-documented. Although the primary motive for our research is to answer questions of a fundamental scientific nature, it is hoped that the results of these studies will provide practical information to the scientific and medical communities to enable more potent and effective ribozyme-based pharmaceuticals to be developed by others. [More]

Scott Publications Bill Scott's E-Mail

Prof Nik SgourakisModelling the Structures of Protein Complexes from Sparse Experimental Data

Nik Sgourakis, Dept. of Chemistry and Biochemistry

Research in the Sgourakis lab focuses on elucidating the structures of important protein complexes involved in Immune recognition of viruses, bacterial secretion and neurodegeneration. Determining the structural basis of protein-protein interactions and self-assembly will help clarify fundamental biological mechanisms and facilitate the design of novel therapeutics. To achieve this, structure-based modelling at sufficient resolution is required. The Sgourakis lab is developing and implementing new tools based on Nuclear Magnetic Resonance spectroscopy and complementary sources of experimental data alongside advanced computational sampling methods. The integration of a range of experimental and computational approaches enables structural studies of proteins and their complexes at high resolution. [More]
Sgourakis Publications Nik Sgourakis' Email

Prof Michael StoneAssembly, Structure, and Regulation of the Telomerase Ribonucleoprotein

Michael Stone, Dept. of Chemistry and Biochemistry

The Stone Research Group combines the use of biochemical and structural methods with newly emerging single-molecule techniques to probe the dynamics of protein-nucleic acid interactions and the molecular mechanisms of biological motors.  Our current area of focus is the structure and function of the telomerase ribonucleoprotein, an RNA-dependent DNA polymerase that maintains genomic stability by synthesizing repetitive DNA sequences at chromosome termini.  These short DNA repeats provide the foundation for specialized chromatin structures, called telomeres, which prevent deleterious chromosome fusion events by differentiating chromosome ends from sites of DNA damage.  It has been shown that telomere length typically decreases with every round of cell division, leading to the so-called ‘molecular clock’ hypothesis, wherein telomere length serves as a signal to control cellular lifespan. This notion is consistent with the finding that active telomere DNA synthesis is normally restricted to rapidly dividing cell types such as stem cells and the majority of human cancers. Our research seeks to elucidate physical mechanisms governing telomere length regulation, and in turn establish a conceptual framework within which to develop novel diagnostic and therapeutic strategies for human disease. [More]

Stone Publications Michael Stone's Email
 

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