Linda Columbus

Last updated
Linda Marie Columbus
Alma mater Scripps Research Institute
University of California, Los Angeles
Smith College
Scientific career
Institutions University of Virginia
Thesis Investigating backbone and side chain dynamics of alpha-helices in the nanosecond regime with site-directed spin labeling  (2001)
Website Columbus Lab

Linda Columbus is an American chemist who is Professor of Chemistry and Molecular Physiology at the University of Virginia. Her research considers the structure-function properties of membrane proteins.

Contents

Early life and education

Columbus was born to young parents, neither of whom were educated beyond high school, and grew up in New Hampshire. [1] Columbus was an undergraduate student at Smith College and moved to the University of California, Los Angeles, for graduate research. [2] Her doctoral research with Prof. Wayne L. Hubbell involved the use of spin labelling to understand the backbone and side chain dynamics of α-helices in the nanosecond regime. [3] After earning her doctorate, Columbus joined The Scripps Research Institute as an NIH research fellow. [4]

Research and career

In 2013, Columbus joined the University of Virginia as an assistant professor. [1] She was promoted to full professor in 2019.[ citation needed ] She studies the membrane proteins that comprise around one quarter of a proteome. These membrane proteins are involved with information transfer across lipid bilayers, and are used as drug targets. [5] Columbus investigates the membrane proteins that mediate interactions between hosts and bacterial pathogens. [4] [6] To study the structures of the membrane proteins involved in cellular invasion by bacterial pathogens, Columbus makes use of site-directed spin labelling and nuclear magnetic resonance. [4] [7]

Awards and honors

Selected publications

Related Research Articles

<span class="mw-page-title-main">Alpha helix</span> Type of secondary structure of proteins

The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located four residues earlier along the protein sequence.

<span class="mw-page-title-main">Transmembrane protein</span> Protein spanning across a biological membrane

A transmembrane protein (TP) is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.

<span class="mw-page-title-main">Lipid raft</span>

The plasma membranes of cells contain combinations of glycosphingolipids, cholesterol and protein receptors organised in glycolipoprotein lipid microdomains termed lipid rafts. Their existence in cellular membranes remains somewhat controversial. It has been proposed that they are specialized membrane microdomains which compartmentalize cellular processes by serving as organising centers for the assembly of signaling molecules, allowing a closer interaction of protein receptors and their effectors to promote kinetically favorable interactions necessary for the signal transduction. Lipid rafts influence membrane fluidity and membrane protein trafficking, thereby regulating neurotransmission and receptor trafficking. Lipid rafts are more ordered and tightly packed than the surrounding bilayer, but float freely within the membrane bilayer. Although more common in the cell membrane, lipid rafts have also been reported in other parts of the cell, such as the Golgi apparatus and lysosomes.

Site-directed spin labeling (SDSL) is a technique for investigating the structure and local dynamics of proteins using electron spin resonance. The theory of SDSL is based on the specific reaction of spin labels with amino acids. A spin label's built-in protein structure can be detected by EPR spectroscopy. SDSL is also a useful tool in examinations of the protein folding process.

<span class="mw-page-title-main">Max Planck Institute of Biochemistry</span>

The Max Planck Institute of Biochemistry (MPIB) is a research institute of the Max Planck Society located in Martinsried, a suburb of Munich. The institute was founded in 1973 by the merger of three formerly independent institutes: the Max Planck Institute of Biochemistry, the Max Planck Institute of Protein and Leather Research, and the Max Planck Institute of Cell Chemistry.

<span class="mw-page-title-main">Max Planck Institute for Biophysical Chemistry</span> Research institute

The Max Planck Institute for Biophysical Chemistry, also known as the Karl-Friedrich Bonhoeffer Institute, was a research institute of the Max Planck Society, located in Göttingen, Germany. On January 1, 2022, the institute merged with the Max Planck Institute for Experimental Medicine in Göttingen to form the Max Planck Institute for Multidisciplinary Sciences.

<span class="mw-page-title-main">Martin Karplus</span>

Martin Karplus is an Austrian and American theoretical chemist. He is the Director of the Biophysical Chemistry Laboratory, a joint laboratory between the French National Center for Scientific Research and the University of Strasbourg, France. He is also the Theodore William Richards Professor of Chemistry, emeritus at Harvard University. Karplus received the 2013 Nobel Prize in Chemistry, together with Michael Levitt and Arieh Warshel, for "the development of multiscale models for complex chemical systems".

<span class="mw-page-title-main">Richard Henderson (biologist)</span>

Richard Henderson is a Scottish molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.

<span class="mw-page-title-main">Molecular biophysics</span> Interdisciplinary research area

Molecular biophysics is a rapidly evolving interdisciplinary area of research that combines concepts in physics, chemistry, engineering, mathematics and biology. It seeks to understand biomolecular systems and explain biological function in terms of molecular structure, structural organization, and dynamic behaviour at various levels of complexity. This discipline covers topics such as the measurement of molecular forces, molecular associations, allosteric interactions, Brownian motion, and cable theory. Additional areas of study can be found on Outline of Biophysics. The discipline has required development of specialized equipment and procedures capable of imaging and manipulating minute living structures, as well as novel experimental approaches.

Wayne L. Hubbell is an American biochemist and member of the National Academy of Sciences. He is Professor of Biochemistry and Jules Stein Professor of Ophthalmology at the University of California, Los Angeles. His research focuses on the visual system, and is primarily supported by a grant from the National Eye Institute.

David S. Cafiso is an American biochemist and a Professor of Chemistry at the University of Virginia. His research focuses on membrane proteins and cell signaling, and is primarily supported by grants from the National Institute of Health.

Harden M. McConnell was an American physical chemist. His many awards included the National Medal of Science and the Wolf Prize, and he was elected to the National Academy of Science."

Protein–lipid interaction is the influence of membrane proteins on the lipid physical state or vice versa.

Michael F. Brown is an American chemist. Since 1987, he has been a Professor of Chemistry at the University of Arizona, and since 2003 has held joint appointments as a Professor of Physics and Professor of Applied Mathematics. Prior to the University of Arizona, Brown earned tenure at the University of Virginia. His research involves the application of NMR spectroscopy and other biophysical methods to study membrane lipids, liquid crystals, and membrane proteins. Brown has particularly been a pioneer in the application of solid-state NMR spectroscopy to the study of lipid bilayer dynamics.

Stephen H. White is an American Biophysicist, academic, and author. He is a Professor Emeritus of Physiology and Biophysics at the University of California, Irvine.

Karen Renee Gibson Fleming is a Professor of Biophysics at Johns Hopkins University. She investigates the energetics of transmembrane helix-helix interactions. Fleming was awarded the 2020 Protein Society Carl Brändén Award.

Jennifer L. Ross is an American physicist who is Professor and Chair of the Department of Physics at Syracuse University. Her research considers active biological condensed matter physics. She was elected Fellow of the American Physical Society in 2018.

Christy F. Landes is an American physical chemist who is the Kenneth S. Pitzer-Schlumberger Chair at Rice University. She seeks to understand the structure-function relationships in biological processes and materials. She was appointed a National Academy of Sciences Kavli Fellow in 2019.

Julie Biteen is a Canadian-born American chemist who is professor of chemistry and biophysics at the University of Michigan. Her research considers the development of imaging systems for biological systems. She was named the Stanford University Sessler Distinguished Alumni Lecturer in 2021.

References

  1. 1 2 "Linda Columbus". The Biophysical Society. Retrieved 2022-04-20.
  2. "Our People". Columbus Lab. Retrieved 2022-04-20.
  3. Columbus, Linda Marie (2001). Investigating backbone and side chain dynamics of [alpha]-helices in the nanosecond regime with site-directed spin labeling. OCLC   732921756.
  4. 1 2 3 "Department of Chemistry". chemistry.as.virginia.edu. Retrieved 2022-04-20.
  5. "Dr. Linda Columbus, University of Virginia". chemistry.umbc.edu. Retrieved 2022-04-20.
  6. "World Changers: Faculty members receive Commonwealth's highest honor". Virginia Magazine. Retrieved 2022-04-20.
  7. "RESEARCH". Columbus Lab. Retrieved 2022-04-20.
  8. "NSF Award Search: Award # 0845668 - CAREER: An Innovative Study of Membrane Protein - Detergent Interactions". www.nsf.gov. Retrieved 2022-04-20.
  9. Advancement, Research Corporation for Science. "CSC Awards". Research Corporation for Science Advancement. Retrieved 2022-04-20.
  10. "CMCP Linda Columbus has received the 2014 Outstanding Faculty Award". Center for Membrane and Cell Physiology. 2014-01-24. Retrieved 2022-04-20.
  11. "Past Council | Biophysical Society". www.biophysics.org. Retrieved 2022-04-20.