Nature 326, 563 - 567 (09 April 1987); doi:10.1038/326563a0

Tests of the helix dipole model for stabilization of -helices

Kevin R. Shoemaker^*, Peter S. Kim^*†, Eunice J. York^‡, John M. Stewart^‡ & Robert L. Baldwin^*

^* Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA
^‡ Department of Biochemistry, University of Colorado School of Medicine, Denver, Colorado 80262, USA
^† Present address: Whitehead Institute, Nine Cambridge Center, Cambridge, Massachusetts 02142, USA.

Charged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1–13 of ribonuclease A) in aqueous solution. One charged-group effect may arise from interactions between charged residues at either end of the helix and the helix dipole. We report here that studies of C-peptide analogues support the helix dipole model, and provide further evidence for the importance of electrostatic interactions not included in the Zimm–Bragg model for -helix formation.

References

1.	Brown, J. E. & Klee, W. A. Biochemistry 10, 470−476 (1971). | Article | PubMed | ISI | ChemPort |
2.	Bierzynski, A., Kim, P.S. & Baldwin, R.L. Proc. natn. Acad. Sci. U.S.A. 79, 2470−2474 (1982). | ChemPort |
3.	Kim, P. S. & Baldwin, R. L. Nature 307, 329−334 (1984). | Article | PubMed | ISI | ChemPort |
4.	Shoemaker, K. R. et al. Proc. natn. Acad. Sci. U.S.A 82, 2349−2353 (1985). | ChemPort |
5.	Zimm, B. H. & Bragg, J. K. J. chem. Phys. 31, 526−535 (1959). | Article | ISI | ChemPort |
6.	Sueki, M. et al. Macromolecules 17, 148−155 (1984). | Article | ChemPort |
7.	Holzwarth, G. & Doty, P. J. Am. chem. Soc. 87, 218−228 (1965). | Article | PubMed | ChemPort |
8.	Mitchinson, C. & Baldwin, R. L. Proteins 1, 23−33 (1986). | Article | PubMed | ChemPort |
9.	Baldwin, R. L. Trends biochem. Sci. 11, 6−9 (1986). | Article | ISI | ChemPort |
10.	Stewart, J. M. & Young, J. D. Solid Phase Peptide Synthesis (Pierce Chemical Company, Rockford, Illinois, 1984).
11.	Wlodawer, A. & Sjölin, L. Biochemistry 22, 2720−2728 (1983). | Article | PubMed | ISI | ChemPort |
12.	Chou, P. Y. & Fasman, G. D. Biochemistry 13, 211−221 (1974). | Article | PubMed | ISI | ChemPort |
13.	Blagdon, D. E. & Goodman, M. Biopolymers 14, 241−245 (1975). | Article | PubMed | ISI | ChemPort |
14.	Ihara, S., Ooi, T. & Takahashi, S. Biopolymers 21, 131−145 (1982). | Article | ChemPort |
15.	Scheraga, H. A. Proc. natn. Acad. Sci. U.S.A. 82, 5585−5587 (1985). | ChemPort |
16.	Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. Nature 273, 443−446 (1978). | Article | PubMed | ISI | ChemPort |
17.	Hol, W. G. J., Halie, L. M. & Sander, C. Nature 294, 532−536 (1981). | Article | PubMed | ISI | ChemPort |
18.	Hol, W. G. J. Prog. Biophys. molec. Biol. 45, 149−195 (1985). | Article | ISI | ChemPort |
19.	Matthew, J. B. A. Rev. Biophys. Biophys. Chem. 14, 387−417 (1985). | ChemPort |
20.	Perutz, M. F., Gronenborn, A. M., Clore, G. M., Fogg, J. H. & Shih, D. T.-b. J. molec. Biol. 183, 491−498 (1985). | Article | PubMed | ISI | ChemPort |
21.	Russu, I. M. & Ho, C. Biochemistry 25, 1706−1716 (1986). | Article | PubMed | ChemPort |
22.	Sheridan, R. P., Levy, R. M. & Salemme, F. R. Proc. natn. Acad. Sci. U.S.A. 79, 4545−4549 (1982). | ChemPort |
23.	Rico, M. et al. Biopolymers 25, 1031−1053 (1986). | Article | PubMed | ChemPort |
24.	Sundaralingam, M., Drendel, W. & Greaser, M. Proc. natn. Acad. Sci. U.S.A. 82, 7944−7947 (1985). | ChemPort |
25.	Maxfield, F. R. & Scheraga, H. A. Macromolecules 8, 491−493 (1975). | Article | PubMed | ChemPort |
26.	Vasquez, M., Pincus, M. R. & Scheraga, H. A. Biopolymers 26, 351−371 (1987). | Article | PubMed | ChemPort |
27.	Pflugrath, J. W. & Quiocho, F. A. Nature 314, 257−260 (1985). | Article | PubMed | ISI | ChemPort |
28.	Chou, P. Y. & Fasman, G. D. Adv. Enzym. 47, 45−148 (1978). | ChemPort |
29.	Bierzynski, A., Dadlez, M., Sobocinska, M. & Kupryszewski, G. Biophys. Chem. 25, 127−134 (1986). | Article | PubMed | ChemPort |