Protein folding roller coaster, one molecule at a time

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 29, 2009, Pages 11823-11824

  Shakhnovich, Eugene ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN G;

BLEACHING; CHROMATOPHORE; FLUORESCENCE RESONANCE ENERGY TRANSFER; NOTE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; TRANSITION TEMPERATURE;

BIOTIN; FLUORESCENCE RESONANCE ENERGY TRANSFER; IMMOBILIZED PROTEINS; KINETICS; PHOTONS; PROTEIN DENATURATION; PROTEIN FOLDING; STREPTAVIDIN; TIME FACTORS; UREA;

EID: 67749106572     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0906228106     Document Type: Note

References (15)

1. Privalov PL, Khechinashvili NN (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J Mol Biol 86:665-684.
2. Abkevich VI, Gutin AM, Shakhnovich EI (1994) Specific nucleus as the transition state for protein folding: Evidence from the lattice model. Biochemistry 33:10026-10036.
3. Ding F, et al. (2002) Direct molecular dynamics observation of protein folding transition state ensemble. Biophys J 83:3525-3532.
4. Klimov DK, Thirumalai D (2001) Multiple protein folding nuclei and the transition state ensemble in two-state proteins. Proteins 43:465-475.
5. Shimada J, Shakhnovich EI (2002) The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation. Proc Natl Acad Sci USA 99:11175-11180.
6. Chung H, Louis J, Eaton, W (2009) Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-byphoton trajectories. Proc Natl Acad Sci USA 106:11837-11844.
7. Talaga DS, et al. (2000) Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc Natl Acad Sci USA 97:13021-13026.
8. Schuler B, Eaton WA (2008) Protein folding studied by single-molecule FRET. Curr Opin Struct Biol 18:16-26.
9. Gin B, Carrahan J, Geissler P (2009) The limited role of non-native contacts in folding pathways of a lattice protein. J Mol Biol, in press.
10. Itzhaki LS, Otzen DE, Fersht AR (1995) The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol 254:260-288.
11. Martinez JC, Pisabarro MT, Serrano L (1998) Obligatory steps in protein folding and the conformational diversity of the transition state. Nat Struct Biol 5:721-729.
12. Kussell E, Shimada J, Shakhnovich EI (2003) Side-chain dynamics and protein folding. Proteins 52:303-321.
13. Goldstein RA, Luthey-Schulten ZA, Wolynes PG (1992) Optimal protein-folding codes from spin-glass theory. Proc Natl Acad Sci USA 89:4918-4922.
14. Ramanathan S, Shakhnovich E (1994) Statistical mechanics of proteins with "evolutionary selected" sequences. Phys Rev E Stat Phys Plasmas Fluids Rel Interdiscip Top 50:1303-1312.
15. Pande VS, Grosberg AY, Tanaka T (1995) Phase diagram of heteropolymers with imprinted conformation. Macromolecules 28:2218-2227.