Kinetics of intramolecular contact formation in a denatured protein

Journal of Molecular Biology

Volumn 332, Issue 1, 2003, Pages 9-12

  Buscaglia, Marco ^a   Schuler, Benjamin ^a,b,c   Lapidus, Lisa J ^a,c   Eaton, William A ^a   Hofrichter, James ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b UNIVERSITY OF POTSDAM   (Germany)

^c STANFORD UNIVERSITY   (United States)

Author keywords

Cold shock protein; Collapse; Triplet state quenching; Unfolded state

Indexed keywords

COLD SHOCK PROTEIN; CYSTEINE; PROTEIN; TRYPTOPHAN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION KINETICS; CONCENTRATION (PARAMETERS); ENERGY TRANSFER; EXPERIMENTAL TEST; LABORATORY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMOTOGA MARITIMA;

THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0041735179     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00891-X     Document Type: Article

References (20)

1. 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol. J. Mol. Biol. 257:1996;669-683.
2. Farrow N.A., Zhang O., Forman-Kay J.D., Kay L.E. Characterization of the backbone dynamics of folded and denatured states of an SH3 domain. Biochemistry. 36:1997;2390-2402.
3. Shortle D., Ackerman M.S. Persistence of native-like topology in a denatured protein in 8 M urea. Science. 293:2001;487-489.
4. Petrescu A.J., Receveur V., Calmettes P., Durand D., Smith J.C. Excluded volume in the configurational distribution of a strongly-denatured protein. Protein Sci. 7:1998;1396-1403.
5. Doniach S. Changes in biomolecular conformation seen by small angle X-ray scattering. Chem. Rev. 101:2001;1763-1778.
6. Millet I.S., Doniach S., Plaxco K.W. Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins. Advan. Protein Chem. 62:2002;241-262.
7. Wilkins D.K., Grimshaw S.B., Dobson C.M., Jones J.A., Smith L.J. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry. 38:1999;16424-16431.
8. Bieri O., Wirz J., Hellrung B., Schutkowski M., Drewello M., Kiefhaber T. The speed limit for protein folding measured by triplet-triplet energy transfer. Proc. Natl Acad. Sci. USA. 96:1999;9597-9601.
9. Hudgins R.R., Huang F., Gramlich G., Nau W.M. A fluorescence-based method for direct measurement of submicrosecond intramolecular contact formation in biopolymers: An exploratory study with polypeptides. J. Am. Chem. Soc. 124:2002;556-564.
10. Neuweiler H., Schulz A., Böhmer M., Enderlein J., Sauer M. Measurement of submicrosecond intramolecular contact formation in peptides at the single-molecule level. J. Am. Chem. Soc. 125:2003;5324-5330.
11. Lapidus L.J., Eaton W.A., Hofrichter J. Measuring the rate of intramolecular contact formation in polypeptides. Proc. Natl Acad. Sci. USA. 97:2000;7220-7225.
12. Lapidus L.J., Eaton W.A., Hofrichter J. Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. Phys. Rev. Letters. 87:2001;. 258101-1-258101-4.
13. Lapidus L.J., Eaton W.A., Hofrichter J. Measuring dynamic flexibility of the coil state of a helix-forming peptide. J. Mol. Biol. 319:2002;19-25.
14. Lapidus L.J., Steinbach P.J., Eaton W.A., Szabo A., Hofrichter J. Effects of chain stiffness on the dynamics of loop formation in polypeptides. Appendix: testing a 1-dimensional diffusion model for peptide dynamics. J. Phys. Chem. ser. B. 106:2002;11628-11640.
15. Gonnelli M., Strambini G.B. Phosphorescence lifetime of tryptophan in proteins. Biochemistry. 34:1995;13847-13857.
16. Perl D., Welker C., Schindler T., Schröder K., Marahiel M.A., Jaenicke R., Schmid F.X. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Struct. Biol. 5:1998;229-235.
17. Welker C., Böhm G., Schurig H., Jaenicke R. Cloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima. Protein Sci. 8:1999;394-403.
18. Schuler B., Lipman E.A., Eaton W.A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature. 419:2002;743-747.
19. Kremer W., Schuler B., Harrieder S., Geyer M., Gronwald W., Welker C., Jaenicke R., Kalbitzer H.R. Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima. Eur. J. Biochem. 268:2001;2527-2539.
20. Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.