Investigation of the nature of the methionine-π interaction in β-hairpin peptide model systems

Protein Science

Volumn 13, Issue 9, 2004, Pages 2515-2522

  Tatko, Chad D ^a   Waters, Marcey L ^a  

^a University of North Carolina at Chapel Hill   (United States)

Author keywords

hairpin peptide; NMR; Noncovalent interactions; Pairwise interactions; Peptide secondary structure; Sulfur aromatic interactions

Indexed keywords

ALANINE DERIVATIVE; AROMATIC AMINO ACID; AROMATIC HYDROCARBON; BETA HAIRPIN PEPTIDE; CATION; CYCLOHEXYLALANINE; METHIONINE; NORLEUCINE; PEPTIDE; PHENYLALANINE; POLYCYCLIC AROMATIC HYDROCARBON DERIVATIVE; SULFUR; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BETA HAIRPIN LOOP; BETA HAIRPIN PEPTIDE MODEL SYSTEM; CATION PI INTERACTION; COMPARATIVE STUDY; HYDROPHOBIC INTERACTION; HYDROPHOBICITY; METHIONINE PI INTERACTION; MODEL; MOLECULAR INTERACTION; NONCOVALENT INTERACTION; NUCLEAR MAGNETIC RESONANCE; PAIRWISE INTERACTION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; THERMODYNAMICS;

AMIDES; HYDROPHOBICITY; MAGNETIC RESONANCE SPECTROSCOPY; METHIONINE; MODELS, MOLECULAR; NORLEUCINE; PEPTIDES; PHENYLALANINE; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SULFUR; THERMODYNAMICS; TRYPTOPHAN;

EID: 4344673535     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04820104     Document Type: Article

References (22)

1. Alber, F., Kuonen, O., Scapozza, L., Folkers, G., and Carloni, P. 1998. Density functional studies on herpes simplex virus type 1 thymidine kinase-substrate interactions: The role of Tyr-172 and Met-128 in thymine fixation. Proteins 31: 453-459.
2. Breinlinger, E.G., Keenan, C.J., and Rotello, V.M. 1998. Modulation of flavin recognition and redox properties through donor atom-π interactions. J. Am. Chem. Soc. 120: 8606-8609.
3. Cheney, B.V., Schulz, M.W., and Cheney, J. 1989. Complexes of benzene with formamide and methanethiol as models for interactions of protein substructures. Biochim. Biophys. Acta 996: 116-124.
4. Gellman, S.H. 1991. On the role of methionine residues in the sequence-independent recognition of nonpolar protein surfaces. Biochemistry 30: 6633-6636.
5. Griffiths-Jones, S.R., Maynard, A.J., Sharman, G.J., and Searle, M.S. 1998. NMR evidence for the nucleation of a β-hairpin peptide conformation in water by an Asn-Gly type I′ β-turn sequence. Chem. Commun. 789-790.
6. Griffiths-Jones, S.R., Maynard, AJ., and Searle, M.S. 1999. Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding. J. Mol. Biol. 292: 1051-1069.
7. Pal, D. and Chakrabarti, P. 1998. Different types of interactions involving cysteine sulfhydryl group in proteins. J. Biomol. Struct. Dyn. 15: 1059-1072.
8. -. 2001. Non-hydrogen bond interactions involving the methionine sulfur atom. J. Biomol. Struct. Dyn. 19: 115-128.
9. Petersen, M.T.N., Jonson, P.H., and Petersen, S.B. 1999. Amino acid neighbours and detailed conformational analysis of cysteines in proteins. Protein Eng. 12: 535-548.
10. Pilger, B.D., Perozzo, R., Alber, F., Wurth, C., Folkers, G., and Scapozza, L. 1999. Substrate diversity of herpes simplex virus thymidine kinase - Impact of the kinematics of the enzyme. J. Biol. Chem. 274: 31967-31973.
11. Reid, K.S.C., Lindley, P.F., and Thornton, J.M. 1985. Sulfur-aromatic interactions in proteins. FEBS Lett. 190: 209-213.
12. Rotello, V.M. 1998. The donor atom-π interaction of sulfur with flavin. A density functional investigation. Heteroatom Chemistry 9: 605-606.
13. Samanta. U., Pal, D., and Chakrabarti, P. 2000. Environment of tryptophan side chains in proteins. Proteins 38: 288-300.
14. Spencer, D.S. and Stiles, W.E. 1996. The M32L substitution of staphylococcal nuclease: Disagreement between theoretical prediction and experimental protein stability. J. Mol. Biol. 257: 497-499.
15. Stapley. B.J., Rohl, C.A., and Doig, A.J. 1995. Addition of side-chain interactions to modified Lifson-Roig helix-coil theory - Application to energetics of phenylalanine-methionine interactions. Protein Sci. 4: 2383-2391.
16. Tatko, C.D. and Waters, M.L. 2002. Selective aromatic interactions in β-hairpin peptides. J. Am. Chem. Soc. 124: 9372-9373.
17. -. 2003. The geometry and efficacy of cation-π interactions in a diagonal position of a designed β-hairpin. Protein Sci. 12: 2443-2452.
18. -. 2004. Comparison of C-H⋯π and hydrophobic interactions in a β-hairpin peptide: Impact on stability and specificity. J. Am. Chem. Soc. 126: 2028-2034.
19. Viguera, A.R. and Serrano, L. 1995. Side-chain interactions between sulfur-containing amino acids and phenylalanine in α-helices. Biochemistry 34: 8771-8779.
20. Wishart, D.S., Sykes, B.D., and Richards, F.M. 1992. The chemical-shift index - A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 1647-1651.
21. Wüthrich, K. 1986. NMR of proteins and nucleic acids. Wiley Interscience Publication, New York.
22. Zauhar, R.J., Colbert, C.L., Morgan, R.S., and Welsh, W.J. 2000. Evidence for a strong sulfur-aromatic interaction derived from crystallographic data. Biopolymers 53: 233-248.