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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.7b01942
|2 doi
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|a pubmed24n0914.xml
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Lin, Shuwei
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Chirality-Driven Parallel and Antiparallel β-Sheet Secondary Structures of Phe-Ala Lipodipeptides
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a Date Completed 16.01.2019
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|a Date Revised 16.01.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Four Phe-Ala lipodipeptides with different stereochemical structures are observed to self-assemble into twisted nanoribbons in water. The handedness of the twisted nanoribbons is controlled by the chirality of the phenylalanine near the alkyl chain, while the stacking handedness of the phenyl and carbonyl groups is determined by the alanine at the C-terminal. The homochiral and heterochiral lipodipeptides self-assemble into parallel and antiparallel β-sheet structures, respectively. The 1H NMR, FTIR, X-ray diffraction, and circular dichroism characterizations indicate that these phenomena are mainly driven by the interaction between neighboring phenyl groups and H-bonding among the amide groups
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Dipeptides
|2 NLM
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|a Lipids
|2 NLM
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|a Phenylalanine
|2 NLM
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|a 47E5O17Y3R
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|a Alanine
|2 NLM
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|a OF5P57N2ZX
|2 NLM
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1 |
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|a Qin, Jiaming
|e verfasserin
|4 aut
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1 |
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|a Li, Yi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Baozong
|e verfasserin
|4 aut
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| 700 |
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|a Yang, Yonggang
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 33(2017), 33 vom: 22. Aug., Seite 8246-8252
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|x 1520-5827
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| 773 |
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|g volume:33
|g year:2017
|g number:33
|g day:22
|g month:08
|g pages:8246-8252
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|u http://dx.doi.org/10.1021/acs.langmuir.7b01942
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