Electronic anisotropy between open shell atoms in first and second order perturbation theory
The interaction between two atoms in states with nonzero electronic orbital angular momenta is anisotropic and can be represented by a spherical tensor expansion. The authors derive expressions for th...
The interaction between two atoms in states with nonzero electronic orbital angular momenta is anisotropic and can be represented by a spherical tensor expansion. The authors derive expressions for th...
Reagents for electrophilic amination: A quantum Monte Carlo study
Electrophilic amination is an appealing synthetic strategy to construct carbon-nitrogen bonds. The authors explore the use of the quantum Monte Carlo method and a proposed variant of the electron pair...
Electrophilic amination is an appealing synthetic strategy to construct carbon-nitrogen bonds. The authors explore the use of the quantum Monte Carlo method and a proposed variant of the electron pair...
On the helix-coil transition in alanine based polypeptides in gas phase
J. Chem. Phys. 126, 204307 (2007); doi:10.1063/1.2734967
Published 24 May 2007
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Using multicanonical simulations, the authors study the effect of charged end groups on helix formation in alanine based polypeptides. They confirm earlier reports that neutral polyalanine exhibits a pronounced helix-coil transition in gas phase simulations. Introducing a charged Lys+ at the C terminal stabilizes the 
helix and leads to a higher transition temperature. On the other hand, adding the Lys+ at the N terminal inhibits helix formation. Instead, a more globular structure was found. These results are in agreement with recent experiments on alanine based polypeptides in gas phase. They indicate that present force fields describe accurately the intramolecular interactions in proteins.
©2007 American Institute of Physics
helix and leads to a higher transition temperature. On the other hand, adding the Lys+ at the N terminal inhibits helix formation. Instead, a more globular structure was found. These results are in agreement with recent experiments on alanine based polypeptides in gas phase. They indicate that present force fields describe accurately the intramolecular interactions in proteins.
©2007 American Institute of Physics
| History: | Received 5 March 2007; accepted 3 April 2007; published 24 May 2007 |
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http://link.aip.org/link/?JCPSA6/126/204307/1 |
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Connotea
CiteULike
del.icio.us
BibSonomy
KEYWORDS and PACS
proteins,
organic compounds,
molecular biophysics,
molecular configurations,
molecular force constants,
ab initio calculations
- 87.15.By
Structure and bonding of biomolecules - 87.15.Kg
Biomolecular interactions; membrane-protein interactions - 87.15.Cc
Folding and sequence analysis of biomolecules - 87.15.Aa
Theory and modeling in molecular biophysics; computer simulation - 87.14.Ee
Proteins - 36.20.Hb
Macromolecular configuration (bonds, dimensions) - YEAR: 2007
RELATED DATABASES
PUBLICATION DATA
0021-9606 (print)
1089-7690 (online)
AIP
REFERENCES (21)
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- P. Dugourd, R. R. Hudgins, D. E. Clemmer, and M. F. Jarrold, Rev. Sci. Instrum. 68, 1122 (1997).
- R. R. Hudgins, J. Woenckhaus, and M. F. Jarrold,
Int. J. Mass Spectrom. Ion Process. 165/166, 497 (1997) . - M. Kohtani, J. E. Schneider, T. C. Jones, and M. F. Jarrold,
J. Am. Chem. Soc. 126, 16981 (2004) . - Y. Peng, U. H. E. Hansmann, and N. A. Alves, J. Chem. Phys. 118, 2374 (2003).
- M. Kohtani and M. F. Jarrold,
J. Am. Chem. Soc. 126, 8454 (2004) . - B. S. Kinnear, D. T. Kaleta, M. Kohtani, R. R. Hudgins, and M. F. Jarrold,
J. Am. Chem. Soc. 122, 9243 (2000) . - Y. Peng and U. H. E. Hansmann,
Biophys. J. 82, 3269 (2002) . - N. A. Alves and U. H. E. Hansmann,
Physica A 292, 509 (2001) . - U. H. E. Hansmann and Y. Okamoto, J. Chem. Phys. 110, 1267 (1999).
- M. J. Sippl, G. Némethy, and H. A. Scheraga,
J. Phys. Chem. 88, 6231 (1984) and references therein. - F. Eisenmenger, U. H. E. Hansmann, Sh. Hayryan, and C.-K. Hu,
Comput. Phys. Commun. 138, 192 (2001) . - F. Eisenmenger, U. H. E. Hansmann, Sh. Hayryan, and C.-K. Hu,
Comput. Phys. Commun. 174, 422 (2006) . - B. A. Berg and T. Neuhaus,
Phys. Lett. B 267, 249 (1991) . - B. A. Berg and T. Celik, Phys. Rev. Lett. 69, 2292 (1992).
- U. H. E. Hansmann and Y. Okamoto,
J. Comput. Chem. 14, 1333 (1993) . - B. A. Berg,
J. Stat. Phys. 82, 323 (1996) . - A. M. Ferrenberg and R. H. Swendsen, Phys. Rev. Lett. 61, 2635 (1988);
- M. Kohtani, T. C. Jones, J. E. Schneider, and M. F. Jarrold,
J. Am. Chem. Soc. 126, 7420 (2004) . - U. H. E. Hansmann, J. Chem. Phys. 120, 417 (2004).
- http://www.ks.uiuc.edu/Research/vmd/
- R. R. Hudgins and M. F. Jarrold,
J. Am. Chem. Soc.121, 3494 (1999) .
