About: Adsorption of Histidine and a Histidine Tripeptide on Au(111) and Au(110) from Acidic Solution

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Adsorption of Histidine and a Histidine Tripeptide on Au(111) and Au(110) from Acidic Solution Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1021/jp307463z
Description	The adsorption of histidine (His), and its peptide glycyl-glycyl-histidine (Gly-Gly-His), on Au(111) and Au(110) has been studied by soft X-ray photoelectron spectroscopy (XPS) and near edge X-ray absorption fine structure spectroscopy (NEXAFS) at the nitrogen and oxygen K-edges. The molecules were adsorbed on surfaces from acidic (pH similar to 3) solution. The results are compared with our previous studies of the adsorption of histidine and its peptides on Au(111) deposited on Au(111) from neutral solutions. When deposited from acidic solution, His adsorbs as carboxylic and carboxylate forms on both Au(111) and Au(110) surfaces, whereas its peptide is present mainly in the carboxylic form. In contrast, both molecules deposited from neutral solution adsorbed mainly as carboxylates. The imino nitrogen atom of the imidazole ring plays a crucial role in the interaction with gold surfaces. The Au 4f core level shift indicates that a chemisorption rather than a physisorption process occurs. The adsorption of histidine (His), and its peptide glycyl-glycyl-histidine (Gly-Gly-His), on Au(111) and Au(110) has been studied by soft X-ray photoelectron spectroscopy (XPS) and near edge X-ray absorption fine structure spectroscopy (NEXAFS) at the nitrogen and oxygen K-edges. The molecules were adsorbed on surfaces from acidic (pH similar to 3) solution. The results are compared with our previous studies of the adsorption of histidine and its peptides on Au(111) deposited on Au(111) from neutral solutions. When deposited from acidic solution, His adsorbs as carboxylic and carboxylate forms on both Au(111) and Au(110) surfaces, whereas its peptide is present mainly in the carboxylic form. In contrast, both molecules deposited from neutral solution adsorbed mainly as carboxylates. The imino nitrogen atom of the imidazole ring plays a crucial role in the interaction with gold surfaces. The Au 4f core level shift indicates that a chemisorption rather than a physisorption process occurs. (en)
Title	Adsorption of Histidine and a Histidine Tripeptide on Au(111) and Au(110) from Acidic Solution Adsorption of Histidine and a Histidine Tripeptide on Au(111) and Au(110) from Acidic Solution (en)
skos:prefLabel	Adsorption of Histidine and a Histidine Tripeptide on Au(111) and Au(110) from Acidic Solution Adsorption of Histidine and a Histidine Tripeptide on Au(111) and Au(110) from Acidic Solution (en)
skos:notation	RIV/00216208:11320/12:10189185!RIV14-MSM-11320___
http://linked.open...avai/predkladatel	Matematicko-fyzikální fakulta
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(LA08022), P(LC06058)
http://linked.open...iv/cisloPeriodika	43
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Tsud, Nataliya
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / Matematicko-fyzikální fakulta
http://linked.open...dnocenehoVysledku	121151
http://linked.open...ai/riv/idVysledku	RIV/00216208:11320/12:10189185
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	base; glycine; photoemission; imidazole; spectroscopy; solid-state; amino-acids; metal-surfaces; electronic-structure; tautomeric equilibria (en)
http://linked.open.../riv/klicoveSlovo	glycine amino-acids metal-surfaces solid-state tautomeric equilibria spectroscopy electronic-structure base photoemission imidazole
http://linked.open...odStatuVydavatele	NL - Nizozemsko
http://linked.open...ontrolniKodProRIV	[3C2641819470]
http://linked.open...i/riv/nazevZdroje	Journal of Physical Chemistry C
http://linked.open...in/vavai/riv/obor	BM
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	Participation of Czech scientists in synchrotron radiation experiments at Elettra Center of synchrotron radiation materials study
http://linked.open...UplatneniVysledku	2012
http://linked.open...v/svazekPeriodika	116
http://linked.open...iv/tvurceVysledku	Tsud, Nataliya Feyer, Vitaliy Iakhnenko, Marianna Plekan, Oksana Prince, Kevin C. Ptasinska, Sylwia
http://linked.open...ain/vavai/riv/wos	000310482900037
issn	1932-7447
number of pages	7 (xsd:int)
http://bibframe.org/vocab/doi	10.1021/jp307463z
http://localhost/t...ganizacniJednotka	11320

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 85 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software