Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales.
Picosecond phase-grating spectroscopy is highly sensitive to density changes and provides a new holographic approach to the study of protein dynamics. Photodissociation of carbon monoxide from heme proteins induces a well-defined transition from a ligated to a deoxy structure that is important to hemoglobin and myoglobin functionality. Grating spectroscopy was used to observe protein-driven density waves on a picosecond time scale after carbon monoxide dissociation. This result demonstrates that global tertiary structure changes of proteins occur on an extremely fast time scale and provides new insight into the biomechanics of deterministic protein motion.
Genberg
L
L
Department of Chemistry, University of Rochester, NY 14627.
Richard
L
L
McLendon
G
G
Miller
R J
RJ
D000818:Animals; D002263:Carboxyhemoglobin / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry*; D066298:In Vitro Techniques; D008024:Ligands; D009038:Motion; D009211:Myoglobin / Q000737:chemistry*; D010108:Oxyhemoglobins / Q000737:chemistry; D013057:Spectrum Analysis / Q000379:methods; D013696:Temperature; D014867:Water / Q000737:chemistry
D006454:Hemoglobins; D008024:Ligands; D009211:Myoglobin; D010108:Oxyhemoglobins; C018013:carboxymyoglobin; D014867:Water; D002263:Carboxyhemoglobin