|
1. George, S. P.; Wang, Y.; Mathew, S.; Srinivasan, K.; Khurana, S. Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders. J. Biol. Chem. 2007, 282, 26528-26541. 2. Vardar, D.; Chishti, A. H.; Frank, B. S.; Luna, E. J.; Noegel, A. A.; Oh, S. W.; Schleicher, M.; McKnight, C. J. Villin-type headpiece domains show a wide range of F-actin-binding affinities. Cell Motil. Cytoskeleton 2002, 52, 9-21. 3. Friederich, E.; Vancompernolle, K.; Louvard, D.; Vandekerckhove, J. Villin function in the organization of the actin cytoskeleton: correlation of in vivo effects to its biochemical activities in vitro. J. Biol. Chem. 1999, 274, 26751-26760. 4. Bazari, W. L.; Matsudaira, P.; Wallek, M.; Smeal, T.; Jakes, R.; Ahmed, Y. Villin sequence and peptide map identify six homologous domains. Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 4986-4990. 5. McKnight, C. J.; Doering, D. S.; Matsudaira, P. T.; Kim, P. S. A thermostable 35-residue subdomain within villin headpiece. J. Mol. Biol. 1996, 260, 126-134. 6. Xiao, S.; Bi, Y.; Shan, B.; Raleigh, D. P. Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain. Biochemistry 2009, 48, 4607-4616. 7. McKnight, C. J.; Matsudaira, P. T.; Kim, P. S. NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Mol. Biol. 1997, 4, 180-184. 8. Žoldák, G.; Stigler, J.; Pelz, B.; Li, H.; Rief, M. Ultrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 18156-18161. 9. Chung, J. K.; Thielges, M. C.; Fayer, M. D. Dynamics of the folded and unfolded villin headpiece (HP35) measured with ultrafast 2D IR vibrational echo spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 3578-3583. 10. Harada, R.; Kitao, A. The fast-folding mechanism of villin headpiece subdomain studied by multiscale distributed computing. J. Chem. Theory Comput. 2012, 8, 290-299. 11. Brewer, S. H.; Vu, D. M.; Tang, Y.; Li, Y.; Franzen, S.; Raleigh, D. P.; Dyer, R. B. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 16662-16667. 12. Tang, Y.; Rigotti, D. J.; Fairman, R.; Raleigh, D. P. Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain. Biochemistry 2004, 43, 3264-3272. 13. Tang, Y.; Goger, M. J.; Raleigh, D. P. NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain. Biochemistry 2006, 45, 6940-6946. 14. Meng, W.; Shan, B.; Tang, Y.; Raleigh, D. P. Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Sci. 2009, 18, 1692-1701. 15. Lindorff-Larsen, K.; Piana, S.; Dror, R. O.; Shaw, D. E. How fast-folding proteins fold. Science 2011, 334, 517-520. 16. Lv, C.; Tan, C.; Qin, M.; Zou, D.; Cao, Y.; Wang, W. Low folding cooperativity of Hp35 revealed by single-molecule force spectroscopy and molecular dynamics simulation. Biophys. J. 2012, 102, 1944-1951. 17. Hocking, H. G.; Häse, F.; Madl, T.; Zacharias, M.; Rief, M.; Žoldák, G. A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain. Biophys. J. 2015, 108, 678-686. 18. Yu, Z.-Q.; Xu, X.-M.; Hong, C.-Y.; Wu, D.-C.; You, Y.-Z. A responsive hyperbranched polymer not only can self-immolate but also can self-cross-link. Macromolecules 2014, 47, 4136-4143. 19. Liu, F.; Goshe, M. B. Combinatorial electrostatic collision-induced dissociative chemical cross-linking reagents for probing protein surface topology. Anal. Chem. 2010, 82, 6215-6223. 20. Churchill, C. D. M.; Eriksson, L. A.; Wetmore, S. D. Formation mechanism and structure of a guanine–uracil DNA intrastrand cross-link. Chem. Res. Toxicol. 2011, 24, 2189-2199. 21. Kennedy-Darling, J.; Smith, L. M. Measuring the formaldehyde protein–DNA cross-link reversal rate. Anal. Chem. 2014, 86, 5678-5681. 22. Jo, H.; Meinhardt, N.; Wu, Y.; Kulkarni, S.; Hu, X.; Low, K. E.; Davies, P. L.; DeGrado, W. F.; Greenbaum, D. C. Development of α-helical calpain probes by mimicking a natural protein–protein interaction. J. Am. Chem. Soc. 2012, 134, 17704-17713. 23. Markiewicz, B. N.; Jo, H.; Culik, R. M.; DeGrado, W. F.; Gai, F. Assessment of local friction in protein folding dynamics using a helix cross-linker. J. Phys. Chem. B 2013, 117, 14688-14696. 24. Merrifield, B. Solid phase synthesis. Science 1986, 232, 341-347. 25. Sigma-Aldrich Co. Basic steps in solid peptide synthesis using Fmoc-chemistry. http://www.sigmaaldrich.com/life-science/custom-oligos/custom-peptides/learning-center/solid-phase-synthesis.html (accessed August 12, 2016). 26. Chan, W. C.; White, P. D. Fmoc solid phase peptide synthesis: a practical approach. Oxford University Press, 2000. 27. Skoog, D. A.; Holler, F. J.; Crouch, S. R. Principles of instrumental analysis. Cengage Learning, 2007. 28. Berova, N.; Nakanishi, K.; Woody, R. W. Circular dichroism: principles and applications. Wiley-VCH, 2000. 29. Fasman, G. D. Circular dichroism and the conformational analysis of biomolecules. Springer US, 1996. 30. Lewars, E. G. Computational chemistry: introduction to the theory and applications of molecular and quantum mechanics. Springer Netherlands, 2011. 31. Cornell, W. D.; Cieplak, P.; Bayly, C. I.; Gould, I. R.; Merz, K. M.; Ferguson, D. M.; Spellmeyer, D. C.; Fox, T.; Caldwell, J. W.; Kollman, P. A. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117, 5179-5197. 32. 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 calculations. J. Comput. Chem. 1983, 4, 187-217. 33. Van Der Spoel, D.; Lindahl, E.; Hess, B.; Groenhof, G.; Mark, A. E.; Berendsen, H. J. C. GROMACS: fast, flexible, and free. J. Comput. Chem. 2005, 26, 1701-1718. 34. Nozaki, Y. The preparation of guanidine hydrochloride. Methods Enzymol. 1972, 26, 43-50. 35. Whitmore, L.; Wallace, B. A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 2008, 89, 392-400. 36. Whitmore, L.; Wallace, B. A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 2004, 32, W668-W673. 37. Wishart, D. S.; Sykes, B. D.; Richards, F. M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 1992, 31, 1647-1651. 38. Glasscock, J. M.; Zhu, Y.; Chowdhury, P.; Tang, J.; Gai, F. Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain. Biochemistry 2008, 47, 11070-11076. 39. Doering, D. S.; Matsudaira, P. Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain. Biochemistry 1996, 35, 12677-12685. 40. Bachem Peptide calculator. http://www.bachem.com/service-support/peptide-calculator (accessed August 23, 2016). 41. Manavalan, P.; Ponnuswamy, P. K. Hydrophobic character of amino acid residues in globular proteins. Nature 1978, 275, 673-674. 42. Nozaki, Y.; Tanford, C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions: establishment of a hydrophobicity scale. J. Biol. Chem. 1971, 246, 2211-2217. 43. Miller, S.; Janin, J.; Lesk, A. M.; Chothia, C. Interior and surface of monomeric proteins. J. Mol. Biol. 1987, 196, 641-656. 44. Fraczkiewicz, R.; Braun, W. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 1998, 19, 319-333. |