Folding of a 16-residue helical peptide using molecular dynamics simulation with Tsallis effective potential
Journal of Chemical Physics, ISSN: 0021-9606, Vol: 111, Issue: 10, Page: 4359-4361
1999
- 36Citations
- 9Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Article Description
We have demonstrated that a molecular dynamics simulation method in conjunction with a Tsallis effective potential enables a 16-residue model peptide to fold into a complete α-helix in a reasonably short time. The current study also indicates that one can practically observe reversible foldings of the peptide with the method, mainly due to its superior capability of overcoming potential energy barriers. Therefore it is anticipated that the new method may provide a quite efficient conformational searching tool for systems with many degrees of freedom such as proteins and DNAs. © 1999 American Institute of Physics.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0000278068&origin=inward; http://dx.doi.org/10.1063/1.480270; https://pubs.aip.org/jcp/article/111/10/4359/294366/Folding-of-a-16-residue-helical-peptide-using; http://aip.scitation.org/doi/10.1063/1.480270; https://aip.scitation.org/action/captchaChallenge?redirectUrl=https%3A%2F%2Faip.scitation.org%2Fdoi%2F10.1063%2F1.480270
AIP Publishing
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