Fast events in protein folding.
Understanding how proteins fold is one of the central problems in biochemistry. A new generation of kinetic experiments has emerged to investigate the mechanisms of protein folding on the previously inaccessible submillisecond time scale. These experiments provide the first glimpse of processes such as secondary structure formation, local hydrophobic collapse, global collapse to compact denatured states, and fast barrier crossings to the native state. Key results are summarized and discussed in terms of the statistical energy landscape theory of protein folding.
Eaton
W A
WA
National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Thompson
P A
PA
Chan
C K
CK
Hage
S J
SJ
Hofrichter
J
J
D001059:Apoproteins / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D001059:Apoproteins; D003574:Cytochrome c Group; D009211:Myoglobin; C010857:apomyoglobin