Relaxations and fluctuations in myoglobin.
One major goal of biological physics is the discovery and understanding of the concepts and laws that govern biomolecules, in particular proteins. Since there exist at least 10(5) different proteins, the choice of a suitable prototype is necessary. Myoglobin (Mb) has for many years played the role of such a prototype. It appears to be simple enough so that many of its properties can be understood, yet it is complex enough to display many of the fascinating characteristics of biomolecules. One major achievement in the study of any protein would be the establishment of convincing connections among structure, kinetics, energy landscape, dynamics, and function. We believe that this goal has not yet been reached in any protein, but the present knowledge of Mb gives some hope that the end is near in this case. Here, we sketch some of the results that have been obtained in the past 50 or more years in the research on Mb, obtained by an army of investigators.
Frauenfelder
H
H
Center for Nonlinear Studies, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. frauenfelder@lanl.gov
McMahon
B H
BH
D007700:Kinetics; D008024:Ligands; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
D008024:Ligands; D009211:Myoglobin