TY - JOUR
T1 - Insights on peptide backbone N-H acidity: Structure of anions, hydration effects
AU - Oliva, Antoni
AU - Henry, Bernard
AU - Ruiz-López, Manuel F.
PY - 2013/3/13
Y1 - 2013/3/13
N2 - Despite the key role played by deamidation reactions in biochemical phenomena such as aging processes, knowledge of factors determining peptide backbone N-H acidities is scarce. We report a theoretical study on this topic by means of quantum-chemical calculations. Gas-phase acidities and pK a's in water have been estimated. The results agree reasonably well with available experimental data. Further analysis suggests that the secondary peptide structure, in addition to hydration effects, is the main factor determining pKa. In particular, we predict N-H protons to be more acidic in β-turns than in α-helices, a finding that may have broad biological implications. © 2013 Elsevier B.V. All rights reserved.
AB - Despite the key role played by deamidation reactions in biochemical phenomena such as aging processes, knowledge of factors determining peptide backbone N-H acidities is scarce. We report a theoretical study on this topic by means of quantum-chemical calculations. Gas-phase acidities and pK a's in water have been estimated. The results agree reasonably well with available experimental data. Further analysis suggests that the secondary peptide structure, in addition to hydration effects, is the main factor determining pKa. In particular, we predict N-H protons to be more acidic in β-turns than in α-helices, a finding that may have broad biological implications. © 2013 Elsevier B.V. All rights reserved.
U2 - 10.1016/j.cplett.2013.01.040
DO - 10.1016/j.cplett.2013.01.040
M3 - Article
VL - 561-562
SP - 153
EP - 158
JO - Chemical Physics Letters
JF - Chemical Physics Letters
SN - 0009-2614
ER -