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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b01194
|2 doi
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|a pubmed25n0954.xml
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|a (NLM)29983068
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Li, Xu
|e verfasserin
|4 aut
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| 245 |
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|a Interchain Overlap Affects Formation of Silk Fibroin Secondary Structures on Hydrophobic Polystyrene Surface Detected via Achiral/Chiral Sum Frequency Generation
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 05.10.2018
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|a Date Revised 05.10.2018
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a Silk fibroin (SF) has been engineered in the biomedical applications on account of its structural robustness, biocompatibility, and biodegradability. However, in situ study is still lacking with respect to the formation of SF secondary structures at the interface. In this paper, by using methanol as an inducing agent, the formation of SF secondary structures at the polystyrene (PS)/SF solution interfaces was detected with achiral and chiral sum frequency generation (SFG) vibrational spectroscopy. SF solutions with two concentrations above and below the critical overlapping concentration ( C*) of SF (∼1.8 mg/mL) were chosen, namely, 90 and 1 mg/mL. We found that above C*, before adding methanol to the protein solution, no ordered SF secondary structures could be detected at the PS/SF solution interface; oppositely, after adding methanol to the protein solution, ordered SF secondary structure, for example, antiparallel β-sheet, could be formed at the PS/protein solution interface. Below C*, both before and after adding methanol to the SF solution, ordered SF secondary structure such as antiparallel β-sheet could be formed. Besides, the addition of methanol could induce the formation of an extended helical structure, verified by the achiral and chiral characteristic bands. Because C* represents a critical solution concentration above which the SF chains can interact with each other and below which the SF chains are isolated in the solution, this achiral/chiral SFG study emphasizes the importance of the chain-chain interaction or spatial confinement on the formation of the protein secondary structures, which provides an additional dimension for the future study of interfacial protein folding
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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1 |
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|a Deng, Guozhe
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ma, Liang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lu, Xiaolin
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 34(2018), 32 vom: 14. Aug., Seite 9453-9459
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:34
|g year:2018
|g number:32
|g day:14
|g month:08
|g pages:9453-9459
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|u http://dx.doi.org/10.1021/acs.langmuir.8b01194
|3 Volltext
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