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 Look Who's at the Lab: Myriam Cotten
In Look Who's at the Lab, we profile some of the hundreds of scientists who visit our lab every year.
Myriam Cotten (center), her students and the
900 MHz NMR magnet.
The Basics
The Research
Quick Q & A
Publications
Title: Assistant Professor, Pacific Lutheran University, Tacoma, Washington
Mag Lab user since: 2000 (in addition to her stint here as a Florida State University graduate student, 1992-1998)
Number of visits to the lab: About 20
Dates of most recent visit: August 2007
Distance traveled: About 3,000 miles (4,828 km)
Research Interests:
"I am genuinely interested in better understanding how atoms and molecules come together to give rise to biological life. The vital roles played by tiny molecules in biological organisms are particularly fascinating to me. Whereas biomolecules rely on a number of common principles to perform a diverse array of functions, multiple parameters such as temperature and concentration modulate the ability of a given biomolecule to contribute its specific function to the organism it belongs to. Shedding light on this intricacy is a core research interest of mine.
"My current research focuses on so-called 'antimicrobial peptides,' which are molecules that help organisms defend themselves against microbes. This is an interdisciplinary field of research that encompasses various aspects of chemistry and biology. Many researchers work in this field with the goal of developing alternatives to the conventional antibiotics that are prone to losing their potency due to bacterial resistance."
Web site: www.chem.plu.edu/cotten/index.html
Email: cottenml@plu.edu
Title: Investigating Molecular Recognition and Biological Function at Interfaces Using Antimicrobial Peptides.
Participants: "In 2006, I came to the lab with four students (pictured above with me, from left to right), Eric Gordon, Breanna Vollmar, Christine Gordon, Randy Saager. In 2007, the group included Elaina Daza, Jeff Ditto, Eric Gordon and Mallorie Taylor. Dr. Riqiang Fu from the Mag Lab is our onsite collaborator."
Synopsis: "At the Magnet Lab, my research group, which typically includes four enthusiastic undergraduate students, collects data that help us understand how antimicrobial peptides perform their function of killing bacteria. We are specifically interested in atomic level information that describe the shape, motions and location of the peptides when they are recognizing and interacting with the types of molecules found on the surface of bacterial cells. Studying peptides under these conditions has the advantage of yielding meaningful information. However, there are many challenges to performing this work due to the complex properties of the samples. This explains why very few antimicrobial peptides have been characterized in this fashion. Our team has been able to contribute to this area of research thanks to the Magnet Lab's solid-state Nuclear Magnetic Resonance capability. This technique shares some principles with clinical Magnetic Resonance Imaging (MRI) and it works very well on our samples. Our multiple visits at the Magnet Lab have allowed us to obtain excellent atomic-level data on piscidin, a novel antimicrobial peptide from fish, so that we can start making connections between its function, shape and motions."
Facility: Nuclear Magnetic Resonance Program, Tallahassee
Equipment: Four solid-state NMR spectrometers (both Wide Bore 600 MHz instruments, the Wide Bore 300 MHz, the Ultra Wide Bore 900 MHz).
Techniques: CP, PISEMA, HETCOR, CP-MAS.
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Favorite thing about working at the lab:
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A:
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I could not pick a single favorite thing because there are so many great things about working at the lab, including the collegial atmosphere, everybody's "yes" attitude, the staff's expertise, and of course the state-of-the-art instruments. |
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Thing you miss most about home when you’re here:
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I miss my husband a lot! I also miss a number of things that are part of everyday life. But I appreciate having a fresh look at them when I come back. It helps catalyze change where it is needed.
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Your proudest science moment:
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Handing in the final version of my Ph. D. dissertation to Dr. Tim Cross, my mentor at FSU/NHMFL. The size of my dissertation (over 300 pages) was a symbol of how enthusiastic I had been about my research projects. It was special to realize that I am not only passionate about using science to investigate our world, but am also dedicated to sharing my passion with others. This moment sowed the seeds from which an academic career started growing for me.
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What keeps you awake at night:
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Wanting to perfect what I am working on!
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The most unscientific thing about you:
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My attraction for the natural world and my aspiration for peace.
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Your hero:
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I have several heroes, including my husband and my parents.
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Last book you read:
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Radiation and Modern Life: Fulfilling Marie Curie's Dream by Alan E. Waltar. It provides interesting perspectives on a controversial topic.
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Parting thoughts on science today:
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How is humanity going to handle climate change and global health? This question is multi-faceted and finding solutions will require a lot of collaboration and creativity at the local and global levels. Being a science professor is very humbling to me because I realize that I teach chemistry to generations of students who will be playing major roles in tackling these questions.
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- R. Fu, M. Truong, R.J. Saager, M. Cotten, and T.A. Cross. High Resolution Heteronuclear Correlation Spectroscopy in Solid State NMR of Aligned Samples. 2007. J. Magn. Reson. 188: 41–48.
- P.L. Gor’kov, E.Y. Chekmenev, C. Li, M. Cotten, J.J. Buffy, N.J. Traaseth, G. Veglia, W.W. Brey. Using Low-E resonators to reduce RF heating in biological samples for static solid-state NMR up to 900 MHz. 2007. J. Magn. Reson. 185: 77–93.
- E.Y. Chekmenev, S.M. Jones, Y.N. Nikolayeva, B.S. Vollmar, T.J. Wagner, P.L. Gor’kov, W.W. Brey, Mc.N. Manion, K.C. Daugherty, and M. Cotten, High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface. 2006. J. Am. Chem. Soc. 128: 5308-5309.
- E.Y. Chekmenev, B.S. Vollmar, K.T. Forseth, McK.N. Manion, S.M. Jones, T.J. Wagner, R.M. Endicott, B.P. Kyriss, L.M. Homem, M. Pate, J. He, J. Raines, P.L. Gor’kov, W.W. Brey, D.J. Mitchell, A.J. Auman, M.J. Ellard-Ivey, J. Blazyk, and M. Cotten. Investigating Molecular Recognition and Biological Function at Interfaces Using Piscidins, Antimicrobial Peptides from Fish. 2006. Invited paper. Biochim. Biophys. Acta. 1758: 1359-1372.
- P.L. Gor’kov, E.Y. Chekmenev, R. Fu, J. Hu, T.A. Cross, M. Cotten, W.W. Brey. A Large Volume Flat Coil Probe for Oriented Membrane Proteins. 2006. J. Magn. Reson. 181: 9-20.
- G. P. Drobny, J. R. Long, W. S. Shaw, M. Cotten, and P. S. Stayton. Studies of Structure and Dynamics of Proteins Adsorbed to Biomaterial Interfaces in Encyclopedia of Nuclear Magnetic Resonance, Advances in NMR, John Wiley & Sons Ltd, NJ. 2002.
- C. D. Cole, A. S. Frost, N. Thompson, M. Cotten, T. A. Cross and D. D. Busath. Noncontact dipole effects on channel permeation. VI. 5F-and 6F-Trp gramicidin channel currents. 2002. Biophys. J. 83: 1974-1986.
- N. Thompson, G. Thompson, C. D. Cole, M. Cotten, T. A. Cross, and D. D. Busath. Noncontact Dipole Effects on Channel Permeation. IV. Kinetic Model of 5F-Trp13 Gramicidin A Currents. 2001. Biophys. J. 81: 1245-1254.
- R. Fu, M. Cotten, and T. A. Cross. 2000. Intermolecular Distance Measurements by Solid State NMR to determine Gramicidin Dimer Structures in Hydrated Phospholipid Bilayers. J Biomol NMR. 16:261-268.
- R. Phillips, C. D. Cole, R. J. Hendershot, M. Cotten, T. A. Cross, D. D. Busath. 1999. Noncontact dipole effects on channel permeation. III. Anomalous proton conductance effects in gramicidin. Biophys J. 77:2492-2501.
- M. Cotten, C. Tian, D. Busath, R. B. Shirts, and T. A. Cross. 1999. Modulating Dipoles for Structure-Function Correlations in the Gramicidin Channel. Biochemistry. 38:9185-9197.
- M. Cotten, R. Fu, and T. A. Cross. 1999. Solid State NMR and Hydrogen Deuterium Exchange in a Bilayer Solubilized Peptide: Structural and Mechanistic Implications. Biophys. J. 76:1179-1189.
- D. A. Busath, C. D. Thulin, R. W. Hendershot, L. R. Revell Philips, P. Maughan, C. D. Cole, N. C. Bingham, S. Morisson, L. C. Baird, R. J. Hendershot, M. Cotten, and T. A. Cross. 1998. Non-Contact Dipole Effects on Channel Permeation. I. Experiments with (5F-Indole) Trp-13 Gramicidin A Channels. Biophys. J. 75:2830-2844.
- M. Cotten, Feng Xu, and T. A. Cross. 1997. Protein Stability and Conformational Rearrangements in Lipid Bilayers: Linear Gramicidins, a Model System. Biophys. J. 73:614-623.
- M. Cotten, V. G. Soghomonian, W. Hu, and T. A. Cross. 1997. High Resolution and High Fields in Biological State NMR. Solid State NMR. 9:77-80.
- V. G. Soghomonian, M. Cotten, R. Rosanske, and T. A. Cross. 1997. Field Stabilization and 2H NMR Spectroscopy in a 24.6 T Resistive Magnet. J. Magn. Reson. 125:212-215.
- S. Aramugam, S. Pascal, C. L. North, W. Hu, K. -C Lee, M. Cotten, R. R. Ketchem, F. Xu., M. Brenneman, F. Kovacs, F. Tian, A. Wang, S. Huo, and T. A. Cross. 1996. Conformational Trapping in a Membrane Environment: a Regulatory Mechanism for Protein Activity. Proc. Natl. Acad. Sci. USA. 93:5872-5876.
Date posted: November 26, 2007
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