{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T02:36:45Z","timestamp":1771036605173,"version":"3.50.1"},"reference-count":86,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2016,9,28]],"date-time":"2016-09-28T00:00:00Z","timestamp":1475020800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Jagiellonian University - Medical College","award":["K\/ZDS\/006363"],"award-info":[{"award-number":["K\/ZDS\/006363"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Entropy"],"abstract":"<jats:p>The aqueous environment is a pervasive factor which, in many ways, determines the protein folding process and consequently the activity of proteins. Proteins are unable to perform their function unless immersed in water (membrane proteins excluded from this statement). Tertiary conformational stabilization is dependent on the presence of internal force fields (nonbonding interactions between atoms), as well as an external force field generated by water. The hitherto the unknown structuralization of water as the aqueous environment may be elucidated by analyzing its effects on protein structure and function. Our study is based on the fuzzy oil drop model\u2014a mechanism which describes the formation of a hydrophobic core and attempts to explain the emergence of amyloid-like fibrils. A set of proteins which vary with respect to their fuzzy oil drop status (including titin, transthyretin and a prion protein) have been selected for in-depth analysis to suggest the plausible mechanism of amyloidogenesis.<\/jats:p>","DOI":"10.3390\/e18100351","type":"journal-article","created":{"date-parts":[[2016,9,28]],"date-time":"2016-09-28T10:56:13Z","timestamp":1475060173000},"page":"351","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Influence of the Aqueous Environment on Protein Structure\u2014A Plausible Hypothesis Concerning the Mechanism of Amyloidogenesis"],"prefix":"10.3390","volume":"18","author":[{"given":"Irena","family":"Roterman","sequence":"first","affiliation":[{"name":"Department of Bioinformatics and Telemedicine, Collegium Medium, Jagiellonian University, Lazarza 16, 31-530 Krakow, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1806-9877","authenticated-orcid":false,"given":"Mateusz","family":"Banach","sequence":"additional","affiliation":[{"name":"Department of Bioinformatics and Telemedicine, Collegium Medium, Jagiellonian University, Lazarza 16, 31-530 Krakow, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Barbara","family":"Kalinowska","sequence":"additional","affiliation":[{"name":"Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, 30-059 Krakow, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Leszek","family":"Konieczny","sequence":"additional","affiliation":[{"name":"Chair of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2016,9,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1126\/science.1219021","article-title":"The protein-folding problem, 50 years on","volume":"338","author":"Dill","year":"2012","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/prot.24452","article-title":"Critical assessment of methods of protein structure prediction (CASP)\u2014Round X","volume":"82","author":"Moult","year":"2014","journal-title":"Proteins"},{"key":"ref_3","unstructured":"Protein Structure Prediction Center. 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