AI Article Synopsis
- The study examined how to accurately determine the interaction energy between Phe20 and a polypeptide complex using different capping strategies and quantum chemical calculations.
- The most reliable results were found when the alpha-amino group was acetylated and the alpha-carbonyl group was methyl amidated, achieving deviations under 10%.
- Other methods involving hydrogenation and methylation were less accurate, with deviations reaching up to 35%, highlighting the importance of choosing capping methods based on structural features and resource availability.
Article Abstract
The accuracy of the determination of the energy of interaction between Phe20 and the Pro5-Thr6-Tyr7-Pro8 complex inside the hydrophobic core of avian pancreatic polypeptide was investigated using three capping strategies for molecular fractionation with conjugated caps and DFT quantum chemical calculations at the BHandHLYP/cc-pVTZ level of theory. The most accurate determination resulted from acetylation of the alpha-amino group combined with methyl amidation of the alpha-carbonyl group with relative deviations less than 10%. Combinations of hydrogenation of the alpha-amino group with the replacement of the alpha-carbonyl group with a hydrogen and the hydrogenation of the alpha-amino group with methylation of the alpha-carbonyl group were less accurate, leading to relative deviations up to 35%. Choice of capping methods depends on the structural features of the polypeptide system, the desired accuracy and the available computational resources.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2577377 | PMC |
| http://dx.doi.org/10.1002/qua.21553 | DOI Listing |
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