Design and characterization of the anion-sensitive coiled-coil peptide

Protein Science

Volumn 6, Issue 7, 1997, Pages 1396-1404

  Hoshino, Masaru ^a   Yumoto, Noboru ^b   Yoshikawa, Susumu ^b   Goto, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b OSAKA NATIONAL RESEARCH INSTITUTE   (Japan)

Author keywords

Anion binding; Leucine zipper; Molten globule; Protein folding; helix

Indexed keywords

ANION; DISULFIDE; GUANIDINE; LEUCINE; LYSINE; PEPTIDE; SODIUM CHLORATE; SOLVENT; VALINE;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY;

EID: 0030743516     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060703     Document Type: Article

References (44)

1. Chakrabartty R, Baldwin RL. 1995. Stability of α-helices. Adv Protein Chem 46:143-176.
2. Chen YH, Yang JT, Martinez HM. 1972. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11:4120-4131.
3. Dill KA, Bromberg S, Yue K, Fiebig KM, Yee DP, Thomas PD, Chan HS. 1995. Principles of protein folding - A perspective from simple exact models. Protein Sci 4:561-602.
4. Goto Y, Aimoto S. 1991. Anion and pH-dependent conformational transition of an amphiphilic polypeptide. J Mol Biol 218:387-396.
5. Goto Y, Calciano LJ, Fink AL. 1990a. Acid-induced folding of proteins. Proc Natl Acad Sci USA 87:573-577.
6. Goto Y, Fink AL. 1994. Acid-induced folding of heme proteins. Methods Enzymol 232:3-15.
7. Goto Y, Hagihara Y. 1992. Mechanism of the conformational transition of melittin. Biochemistry 31:732-738.
8. 2O. Biochemistry 32:11878-11885.
9. Goto Y, Nishikiori S. 1991. Role of electrostatic repulsion in the acidic molten globule of cytochrome c. J Mol Biol 222:679-686.
10. Goto Y, Okamura N, Aimoto S. 1991. ATP-induced conformational transition of denatured proteins. J Biochem Tokyo 109:746-750.
11. Goto Y, Takahashi N, Fink AL. 1990b. Mechanism of acid-induced folding of proteins. Biochemistry 29:3480-3488.
12. Habermann E. 1972. Bee and wasp venoms. Science 177:314-322.
13. Hagihara Y, Aimoto S, Fink AL, Goto Y. 1993. Guanidine hydrochloride-induced folding of proteins. J Mol Biol 231:180-184.
14. Hagihara Y, Kataoka M, Aimoto S, Goto Y. 1992. Charge repulsion in the conformational stability of melittin. Biochemistry 31:11908-11914.
15. Hagihara Y, Oobatake M, Goto Y. 1994a. Thermal unfolding of tetrameric melittin: Comparison with the molten globule state of cytochrome c. Protein Sci 3:1418-1429.
16. Hagihara Y, Tan Y, Goto Y. 1994b. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride. J Mol Biol 237:336-348.
17. Hoshino M, Goto Y. 1994. Perchlorate-induced formation of the alpha-helical structure of mastoparan. J Biochem Tokyo 116:910-915.
18. Kataoka M, Kuwajima K, Tokunaga F, Goto Y. 1997. Structural characterization of the molten globule of α-lactalbumin and a novel approach for discriminating the molten globule by solution X-ray scattering. Protein Sci 6:422-430.
19. Kenar KT, Garcia Moreno B, Freire E. 1995. A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper. Protein Sci 4:1934-1938.
20. Kohn WD, Kay CM, Hodges RS. 1995a. Protein destabilization by electrostatic repulsions in the two-stranded alpha-helical coiled-coil/leucine zipper. Protein Sci 4:237-250.
21. Kohn WD, Monera OD, Kay CM, Hodges RS. 1995b. The effects of interhelical electrostatic repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils. J Biol Chem 270:25495-25506.
22. Lavigne P, Kondejewski LH, Houston ME Jr, Sonnichsen FD, Lix B, Skyes BD, Hodges RS, Kay CM. 1995. Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerizalion. J Mol Biol 254:505-520.
23. Lavigne P, Sonnichsen FD, Kay CM, Hodges RS. 1996. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science 271:1136-1137.
24. Linderstrom-Lang K. 1924. On the ionization of proteins. Compt Rend Trav Lab Carlsberg, Ser Chim 15:1-29.
25. Lumb KJ, Kim PS. 1995. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science 265:436-439.
26. Lumb KJ, Kim PS. 1996. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science 271:1137-1138.
27. Makhatadze GI, Privalov PL. 1995. Energetics of protein structure. Adv Protein Chem 47:307-425.
28. Nakamura H. 1996. Roles of electrostatic interaction in proteins. Quart Rev Biophys 29:1-90.
29. d: Implications for engineering crystals and supramolecular assemblies. Protein Sci 6:80-88.
30. O'Shea EK, Klemm JD, Kim PS, Alber T. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539-544.
31. O'Shea EK, Rutkowski R, Kim PS. 1989. Evidence that the leucine zipper is a coiled coil. Science 243:538-542.
32. O'Shea EK, Rutkowski R, Kim PS. 1992. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell 68:699-708.
33. Pace CN. 1990. Measuring and increasing protein stability. Trends Biotechnol 8:93-98.
34. Privalov PL. 1996. Intermediate states in protein folding. J Mol Biol 255:707-725.
35. Talbot JC, Dufourcq J, de Bony J, Faucon JF, Lussan C. 1979. Conformational change and self association of monomeric melittin. FEBS Lett 102:191-193.
36. Tanford C, Kirkwood J. 1957. Theory of protein transition curves. I. General equations for impenetrable spheres. J Am Chem Soc 79:5333-5339.
37. Terwilliger TC, Eisenberg D. 1982. The structure of melittin. I. Structure determination and partial refinement. J Biol Chem 257:6010-6015.
38. Tompson KS, Vinson CR, Freire E. 1993. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transition factor GCN4. Biochemistry 32:5491-5496.
39. Yang AS, Honig B. 1993. On the pH dependence of protein stability. J Mol Biol 231:459-414.
40. Yu Y, Monera OD, Hodges RS, Privalov PL. 1996. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J Mol Biol 255: 367-372.
41. Zhou NE, Kay CM, Hodges RS. 1994a. The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils. J Mol Biol 237:500-512.
42. Zhou NE, Monera OD, Kay CM, Hodges RS. 1993. Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded a-helical coiled-coil. Biochemistry 32:3178-3187.
43. Zhou NE, Monera OD, Kay CM, Hodges RS. 1994b. α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix. Protein Peptide Lett 1:114-119.
44. Zitzewitz JA, Bilsel O, Luo J, Jones BE, Matthews CR. 1995. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry 34:12812-12819.