AI Article Synopsis
- Avian Pancreatic Polypeptide (aPP) is a 36-residue protein whose stability is primarily influenced by non-bonded interactions rather than the hydrophobic effect.
- Aromatic residues play a crucial role in both local secondary structure stability and the overall tertiary fold stability due to their involvement in various non-bonded interactions.
- Calculations using BHandHLYP/cc-pVTZ reveal that these aromatic interactions contribute significantly to the protein's stability, with energies of weakly polar interactions being comparable to hydrogen bonds.
Article Abstract
Avian Pancreatic Polypeptide is a 36 residue protein that exhibits a tertiary fold. Results of previous experimental and computational studies indicate that the structure of aPP is stabilized more by non-bonded interactions than by the hydrophobic effect. Aromatic residues are known to participate in a variety of long range non-bonded interactions, with both backbone atoms and the atoms of other side-chains, which could be responsible, in part, for the stability of both the local secondary structure and the tertiary fold. The effect of these aromatic interactions on the stability of aPP was calculated using BHandHLYP/cc-pVTZ. Aromatic residues were shown to participate in multiple hydrogen bonded and weakly polar interactions in the secondary structure. The energies of the weakly polar interactions are comparable with those of hydrogen bonds. Aromatic residues were also shown to participate in multiple weakly polar interactions across the tertiary fold, again with energies similar to those of hydrogen bonds.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2577375 | PMC |
| http://dx.doi.org/10.1002/qua.21521 | DOI Listing |
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