Speeding up protein folding: Mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude

Folding and Design

Volumn 2, Issue 1, 1997, Pages 77-87

  Munson, Mary ^a   Anderson, Karen S ^b   Regan, Lynne ^c  

^a YALE UNIVERSITY   (United States)

^b PRINCETON UNIVERSITY   (United States)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Circular dichroism; Fluorescence; Folding kinetics; Protein folding; Stopped flow

Indexed keywords

DITERPENE; ROP;

AMINO ACID SEQUENCE; ARTICLE; AUDIOVISUAL EQUIPMENT; CHEMICAL MODEL; CHEMISTRY; CIRCULAR DICHROISM; KINETICS; MOLECULAR CLONING; MOLECULAR GENETICS; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; CLONING, MOLECULAR; DITERPENES; KINETICS; MODELS, CHEMICAL; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING;

EID: 0030627747     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1359-0278(97)00008-4     Document Type: Article

References (29)

1. Levinthal, C. (1968). Are there pathways for protein folding? J. Chim. Phys. 65, 44-45.
2. Baldwin, R. (1996). Why is protein folding so fast? Proc. Natl. Acad. Sci. USA 93, 2627-2628.
3. Beasty, A., Hurle, M., Manz, J., Stackhouse, T., Onuffer, J. & Matthews, C. (1986). Effects of the phenylalanine-22 → leucine, glutamic acid-49 → methionine, glycine-234 → aspartic acid, and glycine-234 → lysine mutations on the folding and stability of the α subunit of tryptophan synthase from Escherichia coll. Biochemistry 25, 2965-2974.
4. Elöve, G.A., Chaffotte, A.F., Roder, H. & Goldberg, M.E. (1992). Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry 31, 6876-6883.
5. Kim, P. & Baldwin, R. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
6. Jackson, S.E. & Fersht, A.R. (1991). Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30, 10428-10435.
7. Chen, B.-L., Baase, W.A., Nicholson, H. & Schellman, J.A. (1992). Folding kinetics of T4 lysozyme and nine mutants at 12°C. Biochemistry 31, 1464-1476.
8. Serrano, L., Matouschek, A. & Fersht, A. (1992). The folding of an enzyme 111. Structure of the transition state for unfolding of barnase analyzed by a protein engineering procedure. J. Mol. Biol. 224, 805-818.
9. Schindler, T., Herrler, M., Marahiel, M. & Schmid, F. (1995). Extremely rapid protein folding in the absence of intermediates. Nat. Struct. Biol. 2, 663-673.
10. Gittelman, M.S. & Matthews, C.R. (1990). Folding and stability of trp aporepressor from Escherichia coli. Biochemistry 29, 7011-7020.
11. Milla, M.E. & Sauer, R.T. (1994). P22 Arc represser: folding kinetics of a single-domain, dimeric protein. Biochemistry 33, 1125-1133.
12. Wendt, H., Berger, C., Baici, A., Thomas, R.M. & Bosshard, H.R. (1995). Kinetics of folding of leucine zipper domains. Biochemistry 34, 4097-4107.
13. Zitzewitz, J.A., Bilsel, O., Luo, J., Jones, B.E. & Matthews, C.R. (1995). Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry 34, 12812-12819.
14. Waldburger, C., Jonsson, T. & Sauer, R. (1996). Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl. Acad. Sci. USA 93, 2629-2634.
15. Mok, Y.-K., Bycroft, M. & De Prat Gay, G. (1996). The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like. Nat. Struct Biol. 3, 711-717.
16. Cesareni, G. & Banner, D.W. (1985). Regulation of plasmid copy number by complementary RNAs. Trends Biochem. Sci. 17, 303-306.
17. Marino, J.P., Gregorian, R.S., Jr., Csankovszki, G. & Crothers, D.M. (1995). Bent helix formation between RNA hairpins with complementary loops. Science 268, 1448-1454.
18. Munson, M., O'Brien, R., Sturtevant, J.M. & Regan, L (1994). Redesigning the hydrophobic core of a four-helix-bundle protein. Protein Sci. 3, 2015-2022.
19. Munson, M., et al., & Regan, L. (1996). What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Prolein Sci. 5, 1584-1593.
20. Segawa, S.-L., Husimi, Y. & Wada, A. (1973). Kinetics of thermal unfolding of lysozyme. Biopolymers 12, 2521-2537.
21. Dobson, C. & Evans, P. (1984). Protein folding kinetics from magnetization transfer nuclear magnetic resonance. Biochemistry 23, 4267-4270.
22. Milla, M.E., Brown, B.M., Waldburger, C.D. & Sauer, R.T. (1995). P22 Arc pepressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry 34, 13914-13919.
23. Chen, B.-L., Baase, W. & Schellman, J. (1989). Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 28, 691-699.
24. Predki, P.F., Nayak, L.M., Gottlieb, M.B. & Regan, L (1995). Dissecting RNA-protein interactions: RNA-RNA recognition by Rop. Cell 80, 41-50.
25. Burns, J., Butler, J., Moran, J. & Whitesides, G. (1991). Selective reduction of disulfides by tris(2-carboxyethyl) phosphine. J. Org. Chem. 56, 2648-2650.
26. Banner, D., Kokkinidis, M. & Tsernoglou, D. (1987). Structure of the ColE1 Rop protein at 1.7 Å resolution. J. Mol. Biol. 196, 657-675.
27. Munson, M., Predki, P.F. & Regan, L (1994). ColE1-compatible vectors for high-level expression of cloned DNAs from the T7 promoter. Gene 144, 59-62.
28. Tinoco, I., Jr, Sauer, K. & Wang, J. (1985). Physical Chemistry: Principles and Applications in Biological Sciences. Englewood Cliffs, NJ, Prentice-Hall, Inc.
29. Kraulis, P.J. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.