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Phys. Rev. Lett. 94, 128101 (2005) [4 pages]

Picosecond Thermometer in the Amide I Band of Myoglobin

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Robert H. Austin1, Aihua Xie2, Lex van der Meer3, Britta Redlich3, Per-Anker Lindgård4, Hans Frauenfelder5, and Dan Fu6
1Department of Physics, Princeton University, Princeton, New Jersey 08544, USA
2Department of Physics, Oklahoma State University, Stillwater, Oklahoma 74078, USA
3FOM Institute for Plasma Physics, Edisonbaan 14, Nieuwegein, The Netherlands
4Materials Science Department, Risø National Laboratory, DK-4000 Roskilde, Denmark and QUP Centre, Danish Technical University, DK-2800, Lyngby, Denmark
5Theory Division T10, Los Alamos National Laboratory, Los Alamos, New Mexico 87545, USA
6Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA

Received 14 September 2003; revised 11 October 2004; published 28 March 2005

The amide I and II bands in myoglobin show a heterogeneous temperature dependence, with bands at 6.17 and 6.43  μm which are more intense at low temperatures. The amide I band temperature dependence is on the long wavelength edge of the band, while the short wavelength side has almost no temperature dependence. We compare concepts of anharmonic solid-state crystal physics and chemical physics for the origins of these bands. We suggest that the long wavelength side is composed of those amino acids which hydrogen bond to the hydration shell of the protein, and that temperature dependent bands can be used to determine the time it takes vibrational energy to flow into the hydration shell. We determine that vibrational energy flow to the hydration shell from the amide I takes approximately 20 ps to occur.

© 2005 The American Physical Society

URL:
http://link.aps.org/doi/10.1103/PhysRevLett.94.128101
DOI:
10.1103/PhysRevLett.94.128101
PACS:
87.15.Aa