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- aggregation classification "C3".
- aggregation creator person.
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- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 2974577.bibtex.
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- aggregation language "eng".
- aggregation publisher "American Chemical Society (ACS)".
- aggregation rights "I have retained and own the full copyright for this publication".
- aggregation subject "Chemistry".
- aggregation title "Effect of the (n +1) residue on peptide deamidation".
- aggregation abstract "Deamidation occurs spontaneously in peptides and proteins [1]. Many reports show that deamidation has a substantial effect on protein structure, function and stability. An experimental study on pentapeptides [2] shows that Asn deamidation rates are directly related to primary structure near Asn, with a prominent effect from the carboxyl-side (Yyy). We explore the correlation between experimental deamidation rates and primary structure for two pentapeptides (Yyy=Gly, Ile), to identify the factors causing this dependence. A pentapeptide in a water box is subject to Replica-Exchange Molecular Dynamics (REMD) calculations performed with GROMACS 4 software. Furthermore, a succinimide-mediated reaction [3] is investigated with QM/MM calculations utilizing the CP2K code using Nudged-Elastic-Band (NEB) calculations.[p] [p] [p][1] Robinson, NE, Robinson, AB Proc. Natl. Acad. Sci. USA 2001 , 98, 944.[p][2] Robinson, NE J. Peptide Res. 2004 , 63, 426.[p][3] Catak, S., Monard, G., Aviyente, V., Ruiz-López, MF J. Phys. Chem. A 2009 , 113, 1111.".
- aggregation authorList BK240841.
- aggregation endPage "130".
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- aggregation aggregates 4134114.
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