Folding of the Pit1 homeodomain near the speed limit

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

Volumn 108, Issue 2, 2011, Pages 569-573

  Banachewicz, Wiktor ^a   Johnson, Christopher M ^a   Fersht, Alan R ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

Activation energy; Barrier limited; Chevron plot; Dynamics

Indexed keywords

TRANSCRIPTION FACTOR PIT 1; WATER;

ARTICLE; DIFFUSION; ENERGY; FLUORESCENCE; KINETICS; MUTATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; VELOCITY; VISCOSITY;

AMINO ACID SEQUENCE; BIOPHYSICS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SOFTWARE; TEMPERATURE; THERMODYNAMICS; TRANSCRIPTION FACTOR PIT-1; VISCOSITY;

EID: 79551658657     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1017832108     Document Type: Article

References (25)

1. Gianni S, et al. (2003) Unifying features in protein-folding mechanisms. Proc Natl Acad Sci USA 100:13286-13291.
2. Fersht AR, Daggett V (2002) Protein folding and unfolding at atomic resolution. Cell 108:573-582.
3. White GW, et al. (2005) Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding. J Mol Biol 350:757-775.
4. Religa TL, Markson JS, Mayor U, Freund SM, Fersht AR (2005) Solution structure of a protein denatured state and folding intermediate. Nature 437:1053-1056.
5. Religa TL, et al. (2007) The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain. Proc Natl Acad Sci USA 104:9272-9277.
6. Neuweiler H, Banachewicz W, Fersht AR (2010) Kinetics of chain motions within a protein folding intermediate. Proc Natl Acad Sci USA 105:10.1073/pnas.1011666107.
7. Mayor U, et al. (2003) The complete folding pathway of a protein from nanoseconds to microseconds. Nature 421:863-867.
8. McCully ME, Beck DA, Fersht AR, Daggett V (2010) Refolding the engrailed homeodomain: Structural basis for the accumulation of a folding intermediate. Biophys J 99:1628-1636.
9. Kubelka J, Hofrichter J, Eaton WA (2004) The protein folding "speed limit". Curr Opin Struct Biol 14:76-88.
10. Fersht AR, Matouschek A, Serrano L (1992) The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol 224:771-782.
11. Jacobson EM, Li P, Leon-del-Rio A, Rosenfeld MG, Aggarwal AK (1997) Structure of Pit-1 POU domain bound to DNA as a dimer: Unexpected arrangement and flexibility. Genes Dev 11:198-212.
12. Matouschek A, Kellis JT, Jr, Serrano L, Bycroft M, Fersht AR (1990) Transient folding intermediates characterized by protein engineering. Nature 346:440-445. (Pubitemid 120005916)
13. Fersht AR, Wolynes PG (2000) Kinetically significant intermediate in the folding of barnase. Proc Natl Acad Sci USA 97:14121-14126.
14. Gianni S, Ivarsson Y, Jemth P, Brunori M, Travaglini-Allocatelli C (2007) Identification and characterization of protein folding intermediates. Biophys Chem 128:105-113. (Pubitemid 46843445)
15. Jacob M, Schindler T, Balbach J, Schmid FX (1997) Diffusion control in an elementary protein folding reaction. Proc Natl Acad Sci USA 94:5622-5627. (Pubitemid 27241819)
16. Cellmer T, Henry ER, Hofrichter J, Eaton WA (2008) Measuring internal friction of an ultrafast-folding protein. Proc Natl Acad Sci USA 105:18320-18325.
17. Kawahara K, Tanford C (1966) Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J Biol Chem 241:3228-3232.
18. Bai Y, Milne JS, Mayne L, Englander SW (1994) Protein stability parameters measured by hydrogen exchange. Proteins 20:4-14.
19. Cellmer T, Henry ER, Kubelka J, Hofrichter J, Eaton WA (2007) Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration. J Am Chem Soc 129:14564-14565.
20. Banachewicz W (2010) Biophysical Characterization of the Ultrafast Folding Homeodomain - Pit1 (University of Cambridge, Cambridge, UK).
21. Neuweiler H, Johnson CM, Fersht AR (2009) Direct observation of ultrafast folding and denatured state dynamics in single protein molecules. Proc Natl Acad Sci USA 106:18569-18574.
22. Oliveberg M, Tan YJ, Fersht AR (1995) Negative activation enthalpies in the kinetics of protein folding. Proc Natl Acad Sci USA 92:8926-8929.
23. Kubelka J, Chiu TK, Davies DR, Eaton WA, Hofrichter J (2006) Sub-microsecond protein folding. J Mol Biol 359:546-553.
24. Godoy-Ruiz R, et al. (2008) Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data. J Phys Chem B 112:5938-5949.
25. Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (1995) Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21:167-195.