This title appears in the Scientific Report :
2006
Please use the identifier:
http://hdl.handle.net/2128/2375 in citations.
Please use the identifier: http://dx.doi.org/10.1063/1.2364890 in citations.
Side-chain and backbone ordering in a polypeptide
Side-chain and backbone ordering in a polypeptide
We report results from multicanonical simulations of polyglutamic acid chains of length of ten residues. For this simple polypeptide we observe a decoupling of backbone and side-chain ordering in the folding process. While the details of the two transitions vary between the peptide in gas phase and...
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Personal Name(s): | Wei, Y. |
---|---|
Nadler, W. / Hansmann, U. H. E. | |
Contributing Institute: |
John von Neumann - Institut für Computing; NIC |
Published in: | The @journal of chemical physics, 125 (2006) S. 164902 |
Imprint: |
Melville, NY
American Institute of Physics
2006
|
Physical Description: |
164902 |
PubMed ID: |
17092134 |
DOI: |
10.1063/1.2364890 |
Document Type: |
Journal Article |
Research Program: |
Scientific Computing |
Series Title: |
Journal of Chemical Physics
125 |
Subject (ZB): | |
Link: |
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Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1063/1.2364890 in citations.
We report results from multicanonical simulations of polyglutamic acid chains of length of ten residues. For this simple polypeptide we observe a decoupling of backbone and side-chain ordering in the folding process. While the details of the two transitions vary between the peptide in gas phase and in an implicit solvent, our results indicate that, independent of the specific surroundings, upon continuously lowering the temperature side-chain ordering occurs only after the backbone topology is completely formed. |