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Spectroscopy: An International Journal
Volume 27 (2012), Article ID 102423, 8 pages
Impact of β-Turn Sequence on β-Hairpin Dynamics Studied with Infrared-Detected Temperature Jump
1Department of Biophysical Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany
2Department of Chemistry, University of Illinois at Chicago, 845 W. Taylor Street, Chicago, IL 60607-7061, USA
Copyright © 2012 Alexander Popp et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- S. H. Gellman, “Minimal model systems for β sheet secondary structure in proteins,” Current Opinion in Chemical Biology, vol. 2, no. 6, pp. 717–725, 1998.
- N. Schönbrunner, G. Pappenberger, M. Scharf, J. Engels, and T. Kiefhaber, “Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for β-sheet formation,” Biochemistry, vol. 36, no. 29, pp. 9057–9065, 1997.
- W. A. Eaton, V. Muñoz, P. A. Thompson, E. R. Henry, and J. Hofrichter, “Kinetics and dynamics of loops, α-helices, β-hairpins, and fast-folding proteins,” Accounts of Chemical Research, vol. 31, no. 11, pp. 745–753, 1998.
- R. M. Hughes and M. L. Waters, “Model systems for β-hairpins and β-sheets,” Current Opinion in Structural Biology, vol. 16, no. 4, pp. 514–524, 2006.
- J. Zurdo, “Polypeptide models to understand misfolding and amyloidogenesis and their relevance in protein design and therapeutics,” Protein and Peptide Letters, vol. 12, no. 2, pp. 171–187, 2005.
- A. Aguzzi and T. O'Connor, “Protein aggregation diseases: pathogenicity and therapeutic perspectives,” Nature Reviews Drug Discovery, vol. 9, no. 3, pp. 237–248, 2010.
- F. Chiti and C. M. Dobson, “Protein misfolding, functional amyloid, and human disease,” Annual Review of Biochemistry, vol. 75, pp. 333–366, 2006.
- A. G. Cochran, N. J. Skelton, and M. A. Starovasnik, “Tryptophan zippers: stable, monomeric β-hairpins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 10, pp. 5578–5583, 2001.
- S. J. Russell, T. Blandl, N. J. Skelton, and A. G. Cochran, “Stability of cyclic β-hairpins: asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair,” Journal of the American Chemical Society, vol. 125, no. 2, pp. 388–395, 2003.
- S. J. Russell and A. G. Cochran, “Designing stable β-hairpins: energetic contributions from cross-strand residues,” Journal of the American Chemical Society, vol. 122, no. 50, pp. 12600–12601, 2000.
- T. Blandl, A. G. Cochran, and N. J. Skelton, “Turn stability in β-hairpin peptides: investigation of peptides containing 3:5 type I G1 bulge turns,” Protein Science, vol. 12, no. 2, pp. 237–247, 2003.
- J. Kim and T. A. Keiderling, “All-atom molecular dynamics simulations of β-hairpins stabilized by a tight turn: pronounced heterogeneous folding pathways,” Journal of Physical Chemistry B, vol. 114, no. 25, pp. 8494–8504, 2010.
- L. Wu, D. McElheny, R. Huang, and T. A. Keiderling, “Role of tryptophan-tryptophan interactions in Trpzip β-hairpin formation, structure, and stability,” Biochemistry, vol. 48, no. 43, pp. 10362–10371, 2009.
- L. Wu, D. McElheny, T. Takekiyo, and T. A. Keiderling, “Geometry and efficacy of cross-strand Trp/Trp, Trp/Tyr, and Tyr/Tyr aromatic interaction in a β-hairpin peptide,” Biochemistry, vol. 49, no. 22, pp. 4705–4714, 2010.
- A. Roy, P. Bour, and T. A. Keiderling, “TD-DFT modeling of the circular dichroism for a tryptophan zipper peptide with coupled aromatic residues,” Chirality, vol. 21, pp. E163–E171, 2009.
- R. Huang, L. Wu, D. McElheny, P. Bouř, A. Roy, and T. A. Keiderling, “Cross-strand coupling and site-specific unfolding thermodynamics of a trpzip β-Hairpin Peptide using 13C isotopic labeling and IR spectroscopy,” Journal of Physical Chemistry B, vol. 113, no. 16, pp. 5661–5674, 2009.
- K. Hauser, C. Krejtschi, R. Huang, L. Wu, and T. A. Keiderling, “Site-specific relaxation kinetics of a tryptophan zipper hairpin peptide using temperature-jump IR spectroscopy and isotopic labeling,” Journal of the American Chemical Society, vol. 130, no. 10, pp. 2984–2992, 2008.
- T. A. Keiderling and R. A. G. D. Silva, “Conformational studies of peptides with infrared techniques,” in Synthesis of Peptides and Peptidomimetics, M. Goodman and G. Herrman, Eds., pp. 715–738, Georg Thiem, New York, NY, USA, 2002.
- P. I. Haris, “Fourier transform infrared spectroscopic studies of peptides: potentials and pitfalls,” in Proceedings of the Infrared Analysis of Peptides and Proteins: Principles and Applications ACS Symposium Series, B. Ram Singh, Ed., pp. 54–59, ACS, Washington, DC, USA, 2000.
- J. Kubelka and T. A. Keiderling, “Differentiation of β-sheet-forming structures: ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets,” Journal of the American Chemical Society, vol. 123, no. 48, pp. 12048–12058, 2001.
- P. Bour, J. Kubelka, and T. A. Keiderling, “Simulations of oligopeptide vibrational CD: effects of isotopic labeling,” Biopolymers, vol. 53, no. 5, pp. 380–395, 2000.
- C. D. Snow, L. Qiu, D. Du, F. Gai, S. J. Hagen, and V. S. Pande, “Trp zipper folding kinetics by molecular dynamics and temperature-jump spectroscopy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 12, pp. 4077–4082, 2004.
- D. Du, Y. Zhu, C. Y. Huang, and F. Gai, “Understanding the key factors that control the rate of β-hairpin folding,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 45, pp. 15915–15920, 2004.
- W. Y. Yang, J. W. Pitera, W. C. Swope, and M. Gruebele, “Heterogeneous folding of the trpzip hairpin: full atom simulation and experiment,” Journal of Molecular Biology, vol. 336, no. 1, pp. 241–251, 2004.
- L. Wu, D. Mcelheny, V. Setnicka, J. Hilario, and T. A. Keiderling, “Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy,” Proteins, vol. 80, no. 1, pp. 44–60, 2012.
- T. Takekiyo, L. Wu, Y. Yoshimura, A. Shimizu, and T. A. Keiderling, “Relationship between hydrophobic interactions and secondary structure stability for Trpzip β-Hairpin peptides,” Biochemistry, vol. 48, no. 7, pp. 1543–1552, 2009.
- K. Hauser, O. Ridderbusch, A. Roy, A. Hellerbach, R. Huang, and T. A. Keiderling, “Comparison of isotopic substitution methods for equilibrium and t-jump infrared studies of β-hairpin peptide conformation,” Journal of Physical Chemistry B, vol. 114, no. 35, pp. 11628–11637, 2010.
- Y. Xu, R. Oyola, and F. Gai, “Infrared study of the stability and folding kinetics of a 15-residue β-hairpin,” Journal of the American Chemical Society, vol. 125, no. 50, pp. 15388–15394, 2003.
- C. Krejtschi, R. Huang, T. A. Keiderling, and K. Hauser, “Time-resolved temperature-jump infrared spectroscopy of peptides with well-defined secondary structure: a Trpzip β-hairpin variant as an example,” Vibrational Spectroscopy, vol. 48, no. 1, pp. 1–7, 2008.
- W. O. Wray, T. Aida, and R. B. Dyer, “Photoacoustic cavitation and heat transfer effects in the laser-induced temperature jump in water,” Applied Physics B, vol. 74, no. 1, pp. 57–66, 2002.
- C. Krejtschi and K. Hauser, “Stability and folding dynamics of polyglutamic acid,” European Biophysics Journal, vol. 40, no. 5, pp. 673–685, 2011.