End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation (Proceedings of the National Academy of Sciences of the United States of America (2006) 103, (12394-12399) 10.1073/pnas.0604748103);End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation

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

Volumn 103, Issue 33, 2006, Pages 12394-12399

  Möglich, Andreas ^a,b   Joder, Karin ^a   Kiefhaber, Thomas ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

Chain collapse; Chain dynamics; Denaturant; FRET

Indexed keywords

GLYCINE; POLYPEPTIDE; SERINE;

ARTICLE; DIFFUSION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROGEN BOND; HYDROPHOBICITY; MEASUREMENT; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THEORETICAL MODEL;

EID: 33747623305     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0803144105     Document Type: Erratum

References (49)

1. Kuwajima, K. (1989) Proteins Struct. Funct. Genet. 6, 87-103.
2. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E. & Razgulyaev, O. I. (1990) FEBS Lett. 262, 20-24.
3. Eaton, W. A., Thompson, P. A., Chan, C. K., Hagen, S. J. & Hofrichter, J. (1996) Structure (London) 4, 1133-1139.
4. Segel, D., Bachmann, A., Hofrichter, J., Hodgson, K., Doniach, S. & Kiefhaber, T. (1999) J. Mol. Biol. 288, 489-500.
5. Roder, H., Maki, K., Latypov, R. F., Cheng, H. & Shastry, M. C. R. (2005) in Protein Folding Handbook, eds. Buchner, J. & Kiefhaber, T. (Wiley-VCH, Weinheim, Germany), Vol. 1, pp. 491-535.
6. Bachmann, A. & Kiefhaber, T. (2002) Biophys. Chem. 96, 141-151.
7. Dyson, H. J. & Wright, P. E. (2004) Chem. Rev. 104, 3607-3622.
8. Klein-Seetharaman, J., Oikawa, M., Grimshaw, S. B., Wirmer, J., Duchardt, E., Ueda, T., Imoto, T., Smith, L. J., Dobson, C. M. & Schwalbe, H. (2002) Science 295, 1719-1722.
9. Religa, T. L., Markson, J. S., Mayor, U., Freund, S. M. V. & Fersht, A. R. (2005) Nature 437, 1053-1056.
10. Neri, D., Billeter, M., Wider, G. & Wuthrich, K. (1992) Science 257, 1559-1563.
11. Logan, T. M., Theriault, Y. & Fesik, S. W. (1994) J. Mol. Biol. 236, 637-648.
12. Yi, Q., Scalley-Kim, M. L., Alm, E. J. & Baker, D. (2000) J. Mol. Biol. 299, 1341-1351.
13. Kortemme, T., Kelly, M. J., Kay, L. E., Forman-Kay, J. D. & Serrano, L. (2000) J. Mol. Biol. 297, 1217-1229.
14. Wirmer, J., Schlörb, C. & Schwalbe, H. (2005) in Protein Folding Handbook, eds. Buchner, J. & Kiefhaber, T. (Wiley-VCH, Weinheim, Germany), Vol. 2, pp. 737-808.
15. Sanchez, I. E. & Kiefhaber, T. (2003) J. Mol. Biol. 327, 867-884.
16. Pappu, R. V., Srinivasan, R. & Rose, G. D. (2000) Proc. Natl. Acad. Sci. USA 97, 12565-12570.
17. Gong, H., Fleming, P. J. & Rose, G. D. (2005) Proc. Natl. Acad. Sci. USA 102, 16227-16232.
18. Bieri, O., Wirz, J., Hellrung, B., Schutkowski, M., Drewello, M. & Kiefhaber, T. (1999) Proc. Natl. Acad. Sci. USA 96, 9597-9601.
19. Krieger, F., Fierz, B., Bieri, O., Drewello, M. & Kiefhaber, T. (2003) J. Mol. Biol. 332, 265-274.
20. Krieger, F., Fierz, B., Axthelm, F.. Joder, K., Meyer, D. & Kiefhaber, T. (2004) Chem. Phys. 307, 209-215.
21. Krieger, F., Möglich, A. & Kiefhaber, T. (2005) J. Am. Chem. Soc. 127, 3346-3352.
22. Möglich, A., Krieger, F. & Kiefhaber, T. (2005) J. Mol. Biol. 345, 153-162.
23. Schellman, J. A. (1987) Biopolymers 26, 549-559.
24. Schellman, J. A. (2002) Biophys. Chem. 96, 91-101.
25. Förster, T. (1948) Ann. Phys. 2, 55-75.
26. Haas, E., Katchalski-Katzir, E. & Steinberg, I. Z. (1978) Biopolymers 17, 11-31.
27. Lakowicz, J. R., Kusba, J., Wiczk, W., Gryczynski, I. & Johnson, M. L. (1990) Chem. Phys. Lett. 173, 319-326.
28. Lakowicz, J. R., Kusba, J., Gryczynski, I., Wiczk, W., Szmacinski, H. & Johnson, M. L. (1991) J. Phys. Chem. 95, 9654-9660.
29. Haas, E., Wilchek, M., Katchalski-Katzir, E. & Steinberg, I. Z. (1975) Proc. Natl. Acad. Sci. USA 72, 1807-1811.
30. Sadqi, M., Lapidus, L. J. & Munoz, V. (2003) Proc. Natl. Acad. Sci. USA 100, 12117-12122.
31. Weast, R. C., ed. (1972) Handbook of Chemistry and Physics (CRC, Cleveland).
32. Damaschun, G., Damaschun, H., Gast, K. & Zirwer, D. (1998) Biochemistry (Moscow) 63, 259-275.
33. Kohn, J. E., Millett, I. S., Jacob, J., Zagrovic, B., Dillon, T. M., Cingel, N., Dothager, R. S., Seifert, S., Thiyagarajan, P., Sosnick, T. R., et al. (2004) Proc. Natl. Acad. Sci. USA 101, 12491-12496.
34. Schimmel, P. R. & Flory, P. J. (1967) Proc. Natl. Acad. Sci. USA 58, 52-59.
35. Miller, W. G., Brant, D. A. & Flory, P. J. (1967) J. Mol. Biol. 23, 67-80.
36. Flory, P. J. (1969) Statistical Mechanics of Chain Molecules (Hanser, Munich).
37. Fierz, B. & Kiefhaber, T. (2005) in Protein Folding Handbook, eds. Buchner, J. & Kiefhaber, T. (Wiley-VCH, Weinheim, Germany), Vol. 2, pp. 805-851.
38. Baldwin, R. L. (2003) J. Biol. Chem. 278, 17581-17588.
39. Lopez, M., Chin, D.-H., Baldwin, R. L. & Makhatadze, G. I. (2002) Proc. Natl. Acad. Sci. USA 99, 1298-1302.
40. Richardson, J. M., Lopez, M. & Makhatadze, G. I. (2005) Proc. Natl. Acad. Sci. USA 102, 1413-1418.
41. Fersht, A. R. (1987) Trends Biochem. Sci. 12, 301-304.
42. Szabo, A., Schulten, K. & Schulten, Z. (1980) J. Chem. Phys. 72, 4350-4357.
43. Bieri, O. & Kiefhaber, T. (2000) in Protein Folding: Frontiers in Molecular Biology, ed. Pain, R. (Oxford Univ. Press, Oxford), pp. 34-64.
44. Fitzkee, N. C. & Rose, G. D. (2004) Proc. Natl. Acad. Sci. USA 101, 12497-12502.
45. Terazima, M., Okamoto, K. & Hirota, N. (1995) J. Chem. Phys. 102, 2506-2515.
46. von Smoluchowski, M. V. (1917) Z. Phys. Chem. 129-168.
47. Kay, M. S. & Baldwin, R. L. (1996) Nat. Struct. Biol. 3, 439-445.
48. Navon, A., Ittah, V., Landsman, P., Scheraga, H. A. & Haas, E. (2001) Biochemistry 40, 105-118.
49. Pace, C. N. (1986) Methods Enzymol. 131, 266-280.