S. Michael Angel, a professor of chemistry at the University of South Carolina (Columbia, South Carolina), will be presented with the Lester W. Strock Award on Tuesday, October 14, at SciX 2019, in Palm Springs, California.
S. Micheal Angel
S. Michael Angel, a professor of chemistry at the University of South Carolina (Columbia, South Carolina), will be presented with the Lester W. Strock Award on Tuesday, October 14, at SciX 2019, in Palm Springs, California. The award is given by the New England Section of the Society of Applied Spectroscopy in recognition of a selected publication of substantive research or application of analytical atomic spectrochemistry in the fields of earth science, life sciences, or stellar and cosmic sciences.
Angel received his PhD from North Carolina State University and carried out postdoctoral work at the Lawrence Livermore National Laboratory (Livermore, California). His research group focuses on the areas of remote and in situ laser spectroscopy with a focus on deep-ocean, planetary, and homeland security applications of Raman and laser-induced breakdown spectroscopy (LIBS). Among the group’s recent work is the development of a spatial heterodyne Raman spectrometer (SHRS), and exploration of miniature SHS spectrometers for deep UV Raman, remote Raman, and LIBS, underwater LIBS, and for use on future planetary landers and SmallSats.
To see Spectroscopy’s interview with Angel on developing spectroscopy instruments for use in extreme environments, please click here.
Best of the Week: EAS Conference Coverage, IR Spectroscopy, Microplastics
November 22nd 2024Top articles published this week include highlights from the Eastern Analytical Symposium, a news article about the infrared (IR) spectroscopy market, and a couple of news articles recapping spectroscopic analysis of microplastics.
FT-IR Analysis of pH and Xylitol Driven Conformational Changes of Ovalbumin–Amide VI Band Study
November 21st 2024This study uses Fourier transform infrared (FT-IR) spectroscopy to analyze how the globular protein ovalbumin's secondary structures transition under varying pH conditions in the presence of the cosolvent xylitol, highlighting the role of noncovalent interactions in these conformational changes.