Vibrational sum frequency spectroscopy (VSFS) and ab initio density functional theory (DFT) calculations of formic acid on ZnO/Zn have been performed in order to understand the first step of atmospheric corrosion on zinc initiated by formic acid. In addition, infrared reflection absorption spectroscopy (IRAS) has been employed to complement the surface sensitive VSFS results to identify the corrosion products. Oxidized polycrystalline zinc samples were exposed to 120 ppb formic acid in either humid or dry air where, the formic acid adsorption on ZnO/Zn is observed to have a low dependence on the humidity, as deduced by VSFS. Formate is formed on the surface in both dry and humid air and stabilized in configuration after about 90 min exposure in 120 ppb formic acid as seen in the VSFS results. This is evidenced by the occurrence of the CH and symmetric COOvibrations of the formate ion. The DFT calculations support the VSFS results, showing a coordination of the formate to zinc ions without participation from water molecules. † Part of the special section "Physical Chemistry of Environmental Interfaces".

No abstract

(2017) 'Mutantelec : AnIn Silicomutation simulation platform for comparative electrostatic potential proling of proteins.', Journal of computational chemistry., 38 (7). pp. 467-474. Further information on publisher's website:https://doi.org/10.1002/jcc.24712 Publisher's copyright statement: This is the accepted version of the following article: Valdebenito-Maturana, Braulio, Reyes-Suarez, Jose Antonio, Henriquez, Jaime, Holmes, David S., Quatrini, Raquel, Pohl, Ehmke Arenas-Salinas, Mauricio (2017). Mutantelec: AnIn Silicomutation simulation platform for comparative electrostatic potential proling of proteins. Journal of Computational Chemistry 38(7): 467-474, which has been published in nal form at https://doi.org/10.1002/jcc.24712. This article may be used for non-commercial purposes in accordance With Wiley Terms and Conditions for self-archiving. Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 Journal of Computational Chemistry 30The electrostatic potential plays a key role in many biological processes like determining the affinity of a 31 ligand to a given protein target, and they are responsible for the catalytic activity of many enzymes. 32Understanding the effect that amino acid mutations will have on the electrostatic potential of a protein, will

S2 segments) to the gating charge was then obtained by calculating the "electric" displacement of each amino acid side chain in the external field. The results show that the transmembrane electric field is focused inside the voltage sensor domains and that the gating charge arises mainly from the three positively charged residues located on the S4 segment.