Rachel R. Ogorzalek Loo Joins Spectroscopy's Editorial Advisory Board
Spectroscopy is pleased to announce the addition of Rachael R. Ogorzalek Loo to its editorial advisory board.
Spectroscopy
is pleased to announce the addition of Rachel R. Ogorzalek Loo to its editorial advisory board.
Loo is a researcher in the Department of Biological Chemistry at the David Geffen School of Medicine at the University of California Los Angeles (UCLA) She is a member of UCLA’s Department of Energy Laboratory for Genomics and Proteomics and an associate member of the UCLA Molecular Biology Institute.
Her research interests include the development of bioanalytical mass spectrometry methods for the structural characterization of proteins and the elucidation of ionization mechanisms for mass spectrometry. She is also interested in developing the virtual 2D gel method, a matrix-assisted laser desorption and ionization (MALDI) MS-based surface scanning method in which proteins are desorbed directly from polyacrylamide gels for identifying and characterizing protein isoforms and for measuring protein expression profiles from complex biological samples.
Loo is an author of more than 85 scientific publications and currently serves as secretary for the American Society for Mass Spectrometry. She has been a member of various working committees with the Association of Biomedical Resource Facilities. Before joining UCLA, Loo was director of mass spectrometry for the University of Michigan Protein and Carbohydrate Structure Facility, Ann Arbor, Michigan, and later moved to Parke-Davis Pharmaceutical, now part of Pfizer Global Research, also in Ann Arbor, Michigan, as a research associate.
She received her B.S. degree in chemistry from the University of Wisconsin (Madison, Wisconsin), and her PhD degree in physical chemistry from Cornell University (Ithaca, New York). She carried out post-doctoral research at Pacific Northwest National Laboratory, in Richland, Washington.
Getting accurate IR spectra on monolayer of molecules
April 18th 2024Creating uniform and repeatable monolayers is incredibly important for both scientific pursuits as well as the manufacturing of products in semiconductor, biotechnology, and. other industries. However, measuring monolayers and functionalized surfaces directly is. difficult, and many rely on a variety of characterization techniques that when used together can provide some degree of confidence. By combining non-contact atomic force microscopy (AFM) and IR spectroscopy, IR PiFM provides sensitive and accurate analysis of sub-monolayer of molecules without the concern of tip-sample cross contamination. Dr. Sung Park, Molecular Vista, joined Spectroscopy to provide insights on how IR PiFM can acquire IR signature of monolayer films due to its unique implementation.
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