TY - JOUR
T1 - Low-Temperature Spectroscopy
AU - Austin, Robert H.
AU - Erramilli, Shyamsunder
N1 - Funding Information:
The preparation of this chapter was supported by the Officeo f Health and Environmental Research, U.S. Department of Energy. I thank Stephen Cramer, University of California, Davis, John Dawson, University of South Caroline, Louise Heusinkveld, BrookhavenN a-tional Laboratory, Timothy Keiderling, University of Illinois at Chicago, Yu. Sharonov, Engelhardt Institute of Molecular Biology, Moscow, Peter Siddons, Brookhaven National Laboratory, Philip Stephens, Universityo f Southern California,M artin Stillman, University of Western Ontario, and Andrew Thomson, University of East Anglia, for assistance in obtaining preprints, reprints, and references to the current MCD literature.
PY - 1995
Y1 - 1995
N2 - This chapter provides some practical advice on the way to do low-temperature spectroscopy. The chapter discusses the internal structure of visible absorption spectra and their temperature dependence. It also discusses the utilization of low-temperature spectroscopy to probe protein dynamics. The chapter goes beyond the traditional use of low temperatures to trap intermediate chemical states and to speculate the insight that low-temperature spectroscopy provides the role of protein dynamics in controlling chemical reactions. Probably the main reason for the neglect of low-temperature spectroscopy in biophysics is the unstated opinion of many biophysicists that these kinds of studies are irrelevant to the biological aspects of the reaction. Another reason, connected to the first claim of irrelevance, is the fact that any such study of low-temperature dynamics necessarily involves construction of theoretical models, and in complex molecules this is a notoriously difficult and speculative thing to do. Thus, the chapter provides a comprehensive review of all low-temperature studies on biological systems.
AB - This chapter provides some practical advice on the way to do low-temperature spectroscopy. The chapter discusses the internal structure of visible absorption spectra and their temperature dependence. It also discusses the utilization of low-temperature spectroscopy to probe protein dynamics. The chapter goes beyond the traditional use of low temperatures to trap intermediate chemical states and to speculate the insight that low-temperature spectroscopy provides the role of protein dynamics in controlling chemical reactions. Probably the main reason for the neglect of low-temperature spectroscopy in biophysics is the unstated opinion of many biophysicists that these kinds of studies are irrelevant to the biological aspects of the reaction. Another reason, connected to the first claim of irrelevance, is the fact that any such study of low-temperature dynamics necessarily involves construction of theoretical models, and in complex molecules this is a notoriously difficult and speculative thing to do. Thus, the chapter provides a comprehensive review of all low-temperature studies on biological systems.
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U2 - 10.1016/0076-6879(95)46009-8
DO - 10.1016/0076-6879(95)46009-8
M3 - Article
C2 - 7752923
AN - SCOPUS:0028957449
SN - 0076-6879
VL - 246
SP - 131
EP - 168
JO - Methods in enzymology
JF - Methods in enzymology
IS - C
ER -