The Tryptophan/Histidine interaction in α-helices

Journal of Molecular Biology

Volumn 267, Issue 1, 1997, Pages 184-197

  Fernández Recio, Juan ^a   Vázquez, Ana ^b   Civera, Concepción ^b   Sevilla, Paz ^b   Sancho, Javier ^a  

^a UNIVERSITY OF ZARAGOZA   (Spain)

^b UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

Author keywords

Aromatic charged residue interactions; Protein design; Protein folding; Protein stability; helix stability

Indexed keywords

HISTIDINE; PROTEIN; TRYPTOPHAN;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; STATISTICAL ANALYSIS;

EID: 0031582057     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0831     Document Type: Article

References (41)

1. Armstrong K., Fairman R., Baldwin R. L. The (i, i+4) Phe-His interaction studied in an alanine-based α-helix. J. Mol. Biol. 230:1993;284-291.
2. Aue W. P., Bartholdi E., Ernst R. R. Two-dimensional spectroscopy. Application to nuclear magnetic resonance. J. Chem. Phys. 64:1976;2229-2246.
3. Bax A., Davis D. G. Practical aspects of the two dimensional transverse NOE spectroscopy. J. Magn. Reson. 63:1985;207-213.
4. Bradley E. K., Thomason J. F., Cohen F. E., Kosen P. A., Kuntz I. D. Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. J. Mol. Biol. 215:1990;607-622.
5. Chakrabartty A., Kortemme T., Padmanabhan S., Baldwin R. L. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry. 32:1993;5560-5565.
6. Chakrabartty A., Kortemme T., Baldwin R. L. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3:1994;843-852.
7. Chen G. C., Yang J. T. Two point calibration of circular dichrometer with d-10 camphorsulfonic acid. Anal. Letters. 10:1977;1195-1207.
8. Chen Y.-H., Yang J. T., Chau K. H. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry. 13:1974;3350-3359.
9. Dougherty D. A. Cation-π interactions in chemistry and biology: a new view of benzene, phe, tyr, and trp. Science. 271:1996;163-168.
10. Fersht A. Enzyme Structure and Mechanisms. 1985;W. H. Freeman Co, New York.
11. 1H-n.m.r. parameters of the N-terminal 19-residue S-peptide of ribonuclease in aqueous solution. Int. J. Peptide Protein Res. 21:1983;242-253.
12. Gill S. C., von Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
13. Güntert P., Braun W., Wuthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:1991;517-530.
14. Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522-524.
15. Hunter C. A., Sanders J. K. M. The nature of π-π interactions. J. Am. Chem. Soc. 112:1990;5525-5534.
16. Huyghues-Despointes B. M. P., Scholtz J. M., Baldwin R. L. Effect of a single aspartate on the helix stability at different positions in a neutral alanine-based peptide. Protein Sci. 2:1993;1604-1611.
17. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
18. Kippen A. D., Vickery L. A., Fersht A. R. Structural studies on peptides corresponding to mutants of the major α-helix of barnase. Biochemistry. 33:1994;10013-10021.
19. Lifson S., Roig A. On the theory of helix-coil transition in polypeptides. J. Chem. Phys. 34:1961;1963-1974.
20. Loewenthal R., Sancho J., Fersht A. R. Fluorescence spectrum of barnase: contribution of three tryptophan residues and a histidine-related pH dependence. Biochemistry. 30:1991;6775-6779.
21. aand contribution to protein stability. J. Mol. Biol. 224:1992;759-770.
22. Macura S., Ernst R. R. Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. J. Magn. Reson. 63:1980;207-213.
23. Moult J., Unger R. An analysis of protein folding pathways. Biochemistry. 30:1991;3816-3824.
24. Muñoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct. Biol. 1:1994;399-409.
25. Muñoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. J. Mol. Biol. 245:1995;297-308.
26. Muñoz V., Serrano L. Development of the multiple sequence approximation within the AGADIR model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers. 1996.
27. Padmanabhan S., Baldwin R. L. Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i,i +4. J. Mol. Biol. 241:1994;706-713.
28. Rance M. Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J. Magn. Reson. 74:1987;557-564.
29. 1H-NMR data. Biopolymers. 25:1986;1031-1053.
30. Rooman M. J., Koger J. P. A., Wodak S. J. Extracting information on folding from the amino acid sequence: accurate predictions for protein regions with preferred conformations in the absence of tertiary interactions. Biochemistry. 31:1992;10226-10238.
31. as and protein stability. Biochemistry. 31:1992;2253-2258.
32. Scholtz J. M., Qian H., Robbins V. H., Baldwin R. L. The energetics of ion-pair and hydrogen bonding interactions in a helical peptide. Biochemistry. 32:1993;9668-9676.
33. Shalongo W., Stellwagen E. Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction. Protein Sci. 4:1995;1161-1166.
34. Shinitzky M., Goldman R. Fluorometric detection of histidine-tryptophan complexes in peptides and proteins. Eur. J. Biochem. 3:1967;139-144.
35. Singh J., Thornton J. M. Atlas of Protein Side-chain Interactions. 1992;IRL Press, Oxford.
36. Stapley B. J., Rohl C. A., Doig A. J. Addition of side chain interactions to modified Lifson-Roig helix-coil theory: application to energetics of phenylalanine-methionine interactions. Protein Sci. 4:1995;2383-2391.
37. Viguera A. R., Serrano L. Side-chain interactions between sulfur-containing amino acids and phenylalanine in α-helices. Biochemistry. 34:1995;8771-8779.
38. Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graphics. 8:1990;52-56.
39. Vriend G., Sander C., Stouten P. F. W. A novel search method for protein sequence-structure relations using property profiles. Protein Eng. 7:1994;23-29.
40. Wishart D. S., Sykes B. D., Richards F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:1991;311-333.
41. Zimm B. H., Bragg J. K. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:1959;526-535.