{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T19:04:16Z","timestamp":1774638256976,"version":"3.50.1"},"reference-count":50,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2016,8,19]],"date-time":"2016-08-19T00:00:00Z","timestamp":1471564800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"PSC City University of New York"},{"DOI":"10.13039\/100000181","name":"Air Force Office of Scientific Research","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100000181","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2016,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The folding of a recombinant spider silk protein\u2010polymer in the presence of the tri\u2010methylamine osmolytes TMANO and Betaine in 80% H<jats:sub>2<\/jats:sub>O is reported. Circular dichroism measurements (CD) reveal an increase in \u03b1\u2010helical secondary structure with increasing osmolyte concentrations, as determined by an increase in ellipticity at 222 nm. Consistent with this observation, the signal for random coil sampling, observed at 205 nm, is greatly reduced with increasing trimethylamine. Fluorescence spectra of a single tyrosine positioned within the conserved 33\u2010amino acid repeat primary sequence (of the spider\u2010silk mimetic) complements the conformational changes observed by CD. Importantly, there is a correlation between the number of Alkyl\u2010groups (CH<jats:sub>3<\/jats:sub>\u2010) on the amine of the osmolyte and enhanced helicity of the 15\u2010repeat silk\u2010mimetic for the osmolytes tested, ie TMANO, Betaine, Sarcosine and Glycine. These preliminary results are applicable to storing and processing recombinant silk sequences in H<jats:sub>2<\/jats:sub>O, an important mile\u2010stone for widespread use of recombinant silk polymers.<\/jats:p>","DOI":"10.1002\/pro.2995","type":"journal-article","created":{"date-parts":[[2016,8,2]],"date-time":"2016-08-02T23:57:16Z","timestamp":1470182236000},"page":"1853-1862","source":"Crossref","is-referenced-by-count":2,"title":["Folding recombinant spider\u2010silk in H<sub>2<\/sub>O: Effect of osmolytes on the solution conformation of a 15\u2010repeat spider\u2010silk mimetic"],"prefix":"10.1002","volume":"25","author":[{"given":"Glendon D.","family":"McLachlan","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry Queens College CUNY Flushing NY 11367"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Babak","family":"Gandjian","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry Queens College CUNY 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