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Materials Science Division

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Ursula Perez-Salas

Principal Investigator

Materials Science Division; Bldg. 223
Argonne National Laboratory
Argonne IL 60439

Phone: 630-252-8621
Fax: 630-252-7777
Email: perez-salas@anl.gov

Research Interests

My research interests are focused on investigating the physical properties of biological membranes and obtaining structure information on membrane proteins using solutions of lipid mixtures as model systems. Membranes in cells, from the cell's outer wall to the enclosing boundary of the different organelles in the cell, are highly selective barriers. Membranes are mainly impermeable lipid bilayers and their selectivity comes principally from the specific membrane proteins embedded in and spanning the lipid bilayer. Membrane proteins are responsible for the communication between intracellular compartments and between the cell and its environment. Membrane proteins, lipid composition and other associated membrane components, like cholesterol, give a membrane not only its functional specificity, but also leads to specific structural differences that enable their function. As can be seen in the figure below, one obvious structural difference, is that some are folded to form a stacked system while others remain locally extended. Further, these membranes are not structurally static. Local changes are needed, for example, to form or incorporate (fuse) vesicles which are small, spherical, membrane-enclosed compartments responsible for transporting compounds in and out of the cell as well as inside the cell (see figure). Although these structural differences and changes in the membranes of the cell are due to specific composition variations on the plane of the membrane, they can be broadly viewed as being driven by a "softening" process, where the elastic membrane energy is key. Understanding this softening process and how it relates to structure in the plane of the membrane - which ultimately enables its function - is one of my main research interests.

Cell

Model systems that will shed light on the structural differences found in biological membranes are mixed lipid solutions. These have rich phase diagrams, including bicontinuous regimes, from which the physical properties of the bilayer can be extracted by scattering experiments. Complementary techniques like rheology and optical microscopy add to the full characterization and basic understanding of the mixed lipid solutions physical properties. The compositions in these mixed lipid solutions will emulate the compositions found in biological membranes and thus the corresponding results will be extrapolated to the biological membranes. Another exciting aspect of lipid mixture solutions exhibiting the bicontinuous cubic phase, is that they have been recently found to be a promising template for crystallizing membrane proteins (see figure below). In spite of the fact that membrane proteins are encoded by a third of the genes in multi-cellular organisms, the number of proteins whose structure has been obtained lags behind soluble proteins by many orders of magnitude. A clear understanding of the phase behavior of mixed lipid solutions that exhibit the cubic phase will allow the in cubo technique to be used more generally. Control on lipid composition, temperature range and size of the cube unit will make the system very flexible to accommodate many membrane proteins, potentially allowing many more structures to be obtained. At present, the lack of membrane protein structural data obscures our understanding of the biological membrane and slows the development of biotechnologies that would benefit from this knowledge.

in cubo

M. Caffrey, Journal of Structural Biology 142 (2003) 108


Education

1990-1994
Physics (University Medal). Universidad Autónoma Metropolitana, México, (Licenciatura: B.Sc. equivalent).
1994-2000
Ph.D., Chemical Physics. University of Maryland, College Park.

Professional activities

2001-2003
National Research Council Fellow, National Institute of Standards and Technology, Center for Neutron Research. Supervisor Dr. Susan Krueger
2003-2004
Research Physicist, National Institute of Standards and Technology, Center for Neutron Research. Supervisor Dr. Susan Krueger
2004-2006
Project Scientist and instrument responsible of the Advanced Neutron Diffractometer/Reflectometer (ANDR) at the National Institute of Standards and Technology, Center for Neutron Research.
2006-present
Assistant Physicist, Argonne National Laboratory, Argonne, IL.

Awards

1994
University Medal
2001-2003
National Research Council Fellowship

Publications

  • U Perez-Salas, RM Briber, WA Hamilton, MH Rafailovich, J Sokolov, L Nasser.
    Polystyrene network-network interdiffusion.
    MACROMOLECULES 35 (17): 6638-6644 AUG 13 2002
  • U Perez-Salas, RM Briber, MH Rafailovich, J Sokolov.
    Interfacial fracture toughness between glassy polymer networks.
    JOURNAL OF POLYMER SCIENCE PART B-POLYMER PHYSICS 41 (16): 1902-1908 AUG 15 2003
  • UA Perez-Salas, KM Faucher, CF Majkrzak, NF Berk, S Krueger, EL Chaikof.
    Characterization of a biomimetic polymeric lipid bilayer by phase sensitive neutron reflectometry.
    LANGMUIR 19 (19): 7688-7694 SEP 16 2003
  • CF Majkrzak, NF Berk, UA Perez-Salas.
    Phase-sensitive neutron reflectometry.
    LANGMUIR 19 (19): 7796-7810 SEP 16 2003
  • UA Perez-Salas, P Rangan,S Krueger, RM Briber, D Thirumalai, SA Woodson.
    Compaction of a bacterial group I ribozyme coincides with the assembly of core helices.
    BIOCHEMISTRY 43 (6): 1746-1753 FEB 17 2004
  • S Chauhan, G Caliskan, RM Briber, U Perez-Salas, P Rangan, D Thirumalai, SA Woodson.
    RNA tertiary interactions mediate native collapse of a bacterial group I ribozyme.
    JOURNAL OF MOLECULAR BIOLOGY 353 (5): 1199-1209 NOV 11 2005
  • G Caliskan, C Hyeob, U Perez-Salas, RM Briber, SA Woodson, D Thirumalai.
    Semi-flexible polymer distance distribution function reveals a reduction in persistence length in the compaction of a bacterial group I ribozyme by cation condensation.
    PHYSICAL REVIEW LETTERS 95 (26): DEC 31 2005.
  • S Krueger, S Gregurick, J Katsaras, M-P Nieh and UA Perez-Salas.
    SANS from Proteins, Nucleic Acids, Viruses, Micelles and Vesicles.
    Chapter in book: Neutron Scattering and Biology. Springer Biological Physics Series Springer Press, Spring-Verlag, NY. Editors J Fitter, T Gutberlet and J Katsaras. (May 2006)
  • JA Dura, DJ Pierce, CF Majkrzak, NC Maliszewskyj, DJ McGillivray, M Losche, KV O'Donovan, M Mihailescu, U Perez-Salas, DL Worcester, SH White.
    AND/R: Advanced neutron diffractometer/reflectometer for investigation of thin films and multilayers for the life sciences.
    REVIEW OF SCIENTIFIC INSTRUMENTS 77 (7): JUL 2006

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