Stability of secondary structural elements in a solvent-free environment: The α helix

Proteins: Structure, Function and Genetics

Volumn 27, Issue 2, 1997, Pages 165-170

  Kaltashov, Igor A ^a   Fenselau, Catherine ^a  

^a UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

Author keywords

helix; gas phase; kinetic energy release; mass spectrometry; melittin; molecular mechanics; secondary structure

Indexed keywords

METFORMIN;

ALPHA HELIX; ARTICLE; GAS; HYDROGEN BOND; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

MELITTEN; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; SPECTROMETRY, MASS, SECONDARY ION;

EID: 0031056524     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199702)27:2<165::AID-PROT2>3.0.CO;2-F     Document Type: Article

References (40)

1. Cantor, C.R., Schimmel, P.R. "Biophysical Chemistry. "Part I: "The Conformation of Biological Molecules." New York: W.H. Freeman, 1980.
2. Dill, K.A. Dominant forces in protein folding. Biochemistry 29:7133-7155, 1990.
3. Dill, K.A., Bomberg, S., Yue, K., Fiebig, K.M., Yee, D.P., Thomas, P.D., Chan, H.S. Principles of protein folding: A perspective from simple exact models. Protein Sci. 4:561-602, 1995.
4. Fenselau, C. Ion chemistry of biopolymers: Strategies for four sector mass spectrometers. In: "Biomedical Mass Spectrometry: Present and Future." Matsuo, T., Caprioli, R., Gross, M., Seyama, T. (eds.) Chichester, U.K.: John Wiley & Sons, 1994:129-146.
5. Suckau, D., Shi, Y., Beu, S.C., Senko, M.W., Quinn, J.P., Wampler, F.M.III, McLafferty, F.W. Coexisting stable conformations of gaseous protein ions. Proc. Natl. Acad. Sci USA 90:790-793, 1993.
6. Whitehouse, C.M., Dreyer, R.M., Yamashita, M., Fenn, J.B. Electrospray interface for liquid chromatographs and mass spectrometers. Anal Chem. 57:75-679, 1985.
7. Aleksandrov, M.L., Gall, L.N., Krasnov, N.B., Nikolaev, V.I., Pavlenko, V.A., Shkurov, V.A Ion extraction from solutions at atmospheric pressures: A mass spectrometric method of analysis of bioorganic compounds. Dokl. Akad Nauk SSSR 277:379-383, 1984.
8. Karas, M., Hillenkamp, F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 60:2299-2301, 1988.
9. Cheng, X., Fenselau, C. Target capture and ion/molecule reactions in high-energy collisions between protonated polypeptide ions and hydrogen-containing target gases. J. Am. Chem. Soc. 115:10327-10333, 1993.
10. Woods, T.D., Chorush, R.A., Wamper, F.M. III, Little, D.P., O'Connor, P.B., McLafferty, F.W. Gas phase folding and unfolding of cytochrome c cations. Proc. Natl. Acad. Sci. USA 92:2451-2454, 1995.
11. Covey, T., Douglas, D.J. Collision cross sections for protein ions. J. Am. Soc. Mass Spectrom. 4:616-623, 1993.
12. Clemmer, D.E., Hudgings, R.R., Jarrold, M.F. Naked protein conformations: cytochrome c in the gas phase. J. Am. Chem. Soc. 117:10141-10142, 1995.
13. von Helden, G., Wyttenbach, T., Bowers, M.T. Conformation of macromolecules in the gas phase: use of matrix-assisted laser desorption methods in ion chromatography. Science 267:1483-1485, 1995.
14. Wolynes, P.G. Biomolecular folding in vacuo!!!? Proc. Natl. Acad. Sci USA 92:2426-2427, 1995.
15. Kaltashov, I.A., Fenselau, C.C. A direct comparison of "first" and "second" gas phase basicities of the octapeptide RPPGFSPF. J. Am. Chem. Soc. 117:9906-9910, 1995.
16. Adams, J., Strobel, F., Reiter, A. The importance of charge-separation reactions in tandem mass spectrometry of doubly protonated angiotensin II formed by electrospray ionization: experimental consideration and structural implications, J. Am. Soc. Mass Spectrom. 7:30-41, 1996.
17. Dempsey, C.E. The actions of melittin on membranes. Biochim. Biophys Acta 1031:143-161, 1990.
18. Terwilliger, T.C., Eisenberg, D. The structure of melittin. I. Structure determination and partial refinement. J. Biol. Chem. 257:6010-6015, 1982.
19. 1H-NMR study in methanol. Eur. J. Biochem. 173:139-146, 1988.
20. 13C NMR characterization of the structure and dynamics of synthetic melittin and melittin analogues in lipid environments. Biochemistry 31:1301-1313, 1992.
21. Sipos, D., Chandrasekhar, K., Arvidsson, K., Engstrom, A., Ehrenberg, A. Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin: Resonance assignments and secondary structure. Eur. J. Biochem 199:285-291, 1991.
22. Quay, S., Tronson, L.P. Conformational studies of aqueous melittin: Determination of ionization constants of lysine-21 and lysine-23 by reactivity toward 2,4,6-trinitrobenzene-sulfonate. Biochemistry 22:700-707, 1983.
23. Anderegg, R.J., Wagner, D.S., Stevenson, C.L., Borchardt, R.T. The mass spectrometry of helical unfolding in peptides. J. Am. Soc. Mass Spectrom. 5:425-433, 1994.
24. Beynon, J.H., Caprioli, R.M., Baitinger, W.E., Amy, J.W. A new decomposition of a metastable doubly-charged ion in benzene. Org. Mass Spectrom 3:963-965, 1970.
25. Curtis, J.M., Vekey, K., Brenton, A.G., Beynon, J.H. A study of the electron capture induced decompositions and charge separation reactions of the doubly charged isomeric ions of methylpyridines and aniline. Org. Mass Spectrom 22:289-294, 1987.
26. Van Berkel, G.J., McLuckey, S.A., Glish, G.L. Unimolecular and collision-induced reactions of doubly charged porphyrines. J. Am. Soc. Mass Spectrom 3:235-242, 1992.
27. Biemann, K. Contributions of Mass Spectrometry to Peptide and Protein Structure. Biomed. Environ. Mass Spectrom. 16:99-111, 1988.
28. Terwilleger, D.T., Elder, J.F.,Jr., Beynon, J.H., Cooks, R.G. The shapes of metastable peaks. Int. J. Mass Spectrom. Ion Proc. 16:225-242, 1975.
29. Holmes, J.L., Terlouw, J.K. The scope of metastable peak observations. Org. Mass Spectrom. 15:383-396, 1980.
30. Vekey, K., Pocsfalvi, G. Calculation of the kinetic energy release of charge separation process. Org. Mass Spectrom. 27:1203-1209, 1992.
31. Cooks, R.G., Beynon, J.H., Caprioli, R.M., Lester, G.R. Metastable ions Elsevier, New York: 1973.
32. Busman, M., Rockwood, A.L., Smith, R.D. Activation energies for gas-phase dissociations of multiply changed ions from electrospray ionization mass spectrometry. J. Phys. Chem. 96:2397-2400, 1992.
33. McLuckey, S.A., Glish, G.L., Van Berkel, G.L. Charge determination of product ions formed from collision-induced dissociation of multiply protonated molecules via ion/molecule reactions. Anal Chem. 63:1971-1978, 1991.
34. Wu, Z., Fenselau, C. Proton affinity of arginine measured by the kinetic approach. Rapid Comm. Mass Spectrom. 6:403-405, 1992.
35. Wu, Z., Fenselau C. Gas-phase basicities and proton affinities of lysine and histidine measured from the dissociation of proton-bound dimers. Rapid. Comm. Mass Spectrom. 9:777-780, 1994.
36. Brooks, B.R., Bruccoleri, R.E., Olafson, B.D., States, D.J., Swaminathan, S., Karplus, M. CHARMM: a program for macromolecular energy, minimization, and dynamics calculation. J. Comput. Chem. 4:187-217, 1983.
37. Cheng, X., Wu, Z., Fenselau, C. Collision energy dependence of proton-bound dimer dissociation:entropy effects, proton affinities, and intramolecular hydrogen-bonding in protonated peptides. J. Am. Chem. Soc. 115:4844-4848, 1993.
38. Klassen, J.S., Blades, A.T., Kebarle, P. Determination of ion-molecule equilibria involving ions produced by electro-spray, hydration of protonated amines, diamines, and some small peptides. J. Phys. Chem. 99:15509-15517, 1995.
39. Cooks, R.G., Patrie, J.S., Kotiano, T., McLuckey, S.A. Thermochemical determinations by the kinetic method. Mass Spectrom. Rev. 13:287-339, 1994.
40. Rockwood, A.L., Busman, M., Smith, R.D. Coulombic effects in the dissociation of large highly charged ions. Int. J. Mass Spectrom. Ion. Proc. 111:103-129, 1991.