Observation of a dewetting transition in the collapse of the melittin tetramer

Nature

Volumn 437, Issue 7055, 2005, Pages 159-162

  Liu, Pu ^a   Huang, Xuhui ^a   Zhou, Ruhong ^a,b   Berne, B J ^a,b  

^a Howard Hughes Medical Institute   (United States)

^b IBM T J WATSON RESEARCH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBICITY; OLIGOMERS; PHASE TRANSITIONS; VAPORS; WATER;

DEWETTING TRANSITION; HYDROPHOBIC SURFACES; PROTEIN TETRAMERS;

PROTEINS;

ISOLEUCINE; MELITTIN; NANOPARTICLE; OLIGOMER; TETRAMER; WATER; 2,3 DIHYDROXYBIPHENYL OXYGENASE; 2,3-DIHYDROXYBIPHENYL OXYGENASE; DIOXYGENASE;

BIOLOGY;

ARTICLE; COMPUTER SIMULATION; HYDROPHOBICITY; LIQUID; MICROSCOPY; MOLECULAR SIZE; MOLECULE; MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; SCALE UP; VAPOR; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; GENETICS; METABOLISM; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

DIOXYGENASES; HYDROPHOBICITY; MELITTEN; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; WATER;

EID: 24344448662     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature03926     Document Type: Article

References (20)

1. Ball, P. How to keep dry in water. Nature 423, 25-26 (2003).
2. Wallqvist, A. & Berne, B. J. Computer simulation of hydrophobic hydration forces on stacked plates at short range. J. Phys. Chem. 99, 2893-2899 (1995).
3. Hummer, G., Rasaiah, J. R. & Noworyta, J. P. Water conduction through the hydrophobic channel of a carbon nanotube. Nature 414, 188-190 (2001).
4. Leung, K., Luzar, A. & Bratko, D. Dynamics of capillary drying in water. Phys. Rev. Lett. 90, 065502 (2003).
5. Huang, X., Margulis, C. J. & Berne, B. J. The dewetting and collapse of nanoscale hydrophobic objects. Proc. Natl Acad. Sci. USA 100, 11953-11958 (2003).
6. Huang, X., Zhou, R. & Berne, B. J. Drying and hydrophobic collapse of paraffin plates. J. Phys. Chem. B 109, 3546-3552 (2005).
7. Stillinger, F. H. Structure in aqueous solutions of nonpolar solutes from the standpoint of scaled-particle theory. J. Solution Chem. 2, 141-158 (1973).
8. Lum, K., Chandler, D. & Weeks, J. D. Hydrophobicity at small and large length scales. J. Phys. Chem. B 103, 4570-4577 (1999).
9. Chandler, D. Two faces of water. Nature 417, 491 (2002).
10. Sansom, M. S. P. & Biggin, P. C. Biophysics: water at the nanoscale. Nature 414, 156-159 (2001).
11. Zhou, R., Huang, X., Margulius, C. J. & Berne, B. J. Hydrophobic collapse in multidomain protein folding. Science 305, 1605-1609 (2004).
12. Shea, J., Onuchic, J. & Brooks, C. L. Probing the folding free energy landscape of the src-SH3 protein domain. Proc. Natl Acad. Sci. USA 99, 16064-16068 (2002).
13. Cheung, M. S., Garcia, A. E. & Onuchic, J. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc. Natl Acad. Sci. USA 99, 685-690 (2002).
14. Wolde, P. R. T. & Chandler, D. Drying-induced hydrophobic polymer collapse. Proc. Natl Acad. Sci. USA 99, 6539-6543 (2002).
15. Cheng, Y. & Rossky, P. J. Surface topography dependence of biomolecular hydrophobic hydration. Nature 392, 696-699 (1998).
16. Steitz, R. et al. Nanobubbles and their precursor layer at the interface of water against a hydrophobic substrate. Langmuir 19, 2409-2418 (2003).
17. Jensen, T. R. et al. Water in contact with extended hydrophobic surfaces: Direct evidence of weak dewetting. Phys. Rev. Lett. 90, 086101 (2003).
18. Terwilliger, T. C. & Eisenberg, D. The structure of melittin. J. Biol. Chem. 257, 6010-6015 (1982).
19. Jorgensen, W. L., Maxwell, D. & Tirado-Rives, J. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118, 11225-11236 (1996).
20. Lindahl, E., Hess. B. & van der Spoel, D. Gromacs 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Model. 7, 306-317 (2001).