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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1021/la101413e
|2 doi
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|a pubmed24n0664.xml
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|a DE-627
|b ger
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|e rakwb
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|a eng
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|a Rampulla, David M
|e verfasserin
|4 aut
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|a Higher-order complexity through R-group effects in self-assembled tripeptide monolayers
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|c 2010
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 07.02.2011
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|a Date Revised 21.11.2013
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|a published: Print
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|a Citation Status MEDLINE
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|a Self-assembled monolayers of tri-L-leucine and tri-L-valine formed on highly ordered pyrolytic graphite (HOPG) substrates have been examined using scanning tunneling microscopy. These monolayers exhibit markedly different structures, even though the tripeptides differ by only a minor change in the amino acid R-group. This minor change in R-group apparently affects the balance between hydrogen bonding and van der Waals interactions that control the monolayer structures. Implications of this effect for evolution of molecular complexity in prebiotic synthesis on environmental surfaces are discussed
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Membranes, Artificial
|2 NLM
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|a Oligopeptides
|2 NLM
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|a pyrolytic carbon
|2 NLM
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|a Carbon
|2 NLM
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|a 7440-44-0
|2 NLM
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|a Leucine
|2 NLM
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|a GMW67QNF9C
|2 NLM
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|a Valine
|2 NLM
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|a HG18B9YRS7
|2 NLM
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|a Oncel, Nuri
|e verfasserin
|4 aut
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|a Malcolm, Stuart A
|e verfasserin
|4 aut
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|a Bernasek, Steven L
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 26(2010), 21 vom: 02. Nov., Seite 16287-90
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:26
|g year:2010
|g number:21
|g day:02
|g month:11
|g pages:16287-90
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|u http://dx.doi.org/10.1021/la101413e
|3 Volltext
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