Picosecond thermometer in the amide I band of myoglobin.
The amide I and II bands in myoglobin show a heterogeneous temperature dependence, with bands at 6.17 and 6.43 microm 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.
Austin
Robert H
RH
Department of Physics, Princeton University, Princeton, New Jersey 08544, USA.
Xie
Aihua
A
van der Meer
Lex
L
Redlich
Britta
B
Lindgård
Per-Anker
PA
Frauenfelder
Hans
H
Fu
Dan
D
D000577:Amides / Q000737:chemistry; D000818:Animals; D006860:Hydrogen Bonding; D009211:Myoglobin / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013696:Temperature; D013816:Thermodynamics; D014907:Whales
D000577:Amides; D009211:Myoglobin