TY - JOUR
T1 - Protein folding
T2 - The free energy surface
AU - Gruebele, Martin
N1 - Funding Information:
The author was supported by grant R01 GM057175 from the National Institutes of Health.
PY - 2002/4/1
Y1 - 2002/4/1
N2 - Quantitative models and experiments are revealing how the folding free energy surface of a protein is sculpted by sequence and environment. The sometimes conflicting demands of folding, structure and function determine which folding pathways, if any, dominate. Recent advances include experimental estimates of diffusive barrier-crossing times, the observation of ultrafast folders amenable to full-atom simulation, the use of thermodynamic tuning and nonconservative mutations to probe 'hidden' parts of the free energy surface, and a complete microscopic theory of folding.
AB - Quantitative models and experiments are revealing how the folding free energy surface of a protein is sculpted by sequence and environment. The sometimes conflicting demands of folding, structure and function determine which folding pathways, if any, dominate. Recent advances include experimental estimates of diffusive barrier-crossing times, the observation of ultrafast folders amenable to full-atom simulation, the use of thermodynamic tuning and nonconservative mutations to probe 'hidden' parts of the free energy surface, and a complete microscopic theory of folding.
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U2 - 10.1016/S0959-440X(02)00304-4
DO - 10.1016/S0959-440X(02)00304-4
M3 - Review article
C2 - 11959492
AN - SCOPUS:0036535895
SN - 0959-440X
VL - 12
SP - 161
EP - 168
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 2
ER -