The interaction of thiocyanate with peptides-A computational study
© 2024 Wiley Periodicals LLC.
| Publié dans: | Journal of computational chemistry. - 1984. - 45(2024), 26 vom: 05. Okt., Seite 2214-2231 |
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| Auteur principal: | |
| Autres auteurs: | |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2024
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| Accès à la collection: | Journal of computational chemistry |
| Sujets: | Journal Article density functional theory model peptides protein denaturation thiocyanate Thiocyanates Peptides O748SU14OM |
| Résumé: | © 2024 Wiley Periodicals LLC. According to the Hofmeister series, thiocyanate is the strongest "salting in" anion. In fact, it has a strong denaturant activity against the native state of globular proteins. A molecular level rationalization of the Hofmeister series is still missing, and therefore the denaturant activity of thiocyanate also awaits a robust explanation. In the last years, different types of experimental studies have shown that thiocyanate is capable to directly interact with both polar and nonpolar groups of polypeptide chains. This finding has been scrutinized via a careful computational procedure based on density functional theory approaches. The results indicate that thiocyanate is able to make H-bonds via both the nitrogen and sulfur atom, and to make strong van der Waals interactions with almost all the groups of polypeptide chains, regardless of their polarity |
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| Description: | Date Completed 09.08.2024 Date Revised 09.08.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1096-987X |
| DOI: | 10.1002/jcc.27440 |