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231224s2013 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1021/la400910g
|2 doi
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|a pubmed24n0756.xml
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|e rakwb
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|a eng
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| 100 |
1 |
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|a Fu, Yitai
|e verfasserin
|4 aut
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1 |
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|a Terminal is important for the helicity of the self-assemblies of dipeptides derived from alanine
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|c 2013
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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 11.12.2013
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|a Date Revised 21.05.2013
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The organization of peptides and proteins attracts much attention, due to the biofunctionalities of the self-assemblies. Herein, four dipeptides derived from alanine were synthesized. It was found that the handedness of their self-assemblies was controlled by the chirality of the alanines at the terminals. The organic self-assemblies were studied using circular dichroism, (1)H NMR, Fourier transform infrared, field-emission electron microscopy, transmission electron microscopy, and X-ray diffraction. The results indicated that the electrostatic interactions among the carboxylate groups and H-bondings among the amide groups at the terminals play important roles in the formation of the organic self-assemblies
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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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| 650 |
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|a Alanine
|2 NLM
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| 650 |
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|a OF5P57N2ZX
|2 NLM
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| 700 |
1 |
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|a Li, Baozong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Huang, Zhibin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Yi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yang, Yonggang
|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 1992
|g 29(2013), 20 vom: 21. Mai, Seite 6013-7
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:29
|g year:2013
|g number:20
|g day:21
|g month:05
|g pages:6013-7
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|u http://dx.doi.org/10.1021/la400910g
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