About: Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry

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About: Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry 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/ac404076j
Description	Hydrogen/deuterium exchange coupled to mass spectrometry (HXMS) utilizes enzymatic digestion of proteins to localize the information about altered exchange patterns in protein structure. The ability of the protease to produce small peptides and overlapping fragments and provide sufficient coverage of the protein sequence is essential for localizing regions of interest. Recently, it was shown that there is an interesting group of proteolytic enzymes from carnivorous pitcher plants of the genus Nepenthes. In this report, we describe successful immobilization and the use of one of these enzymes, nepenthesin-1, in HXMS workflow. In contrast to pepsin, it has different cleavage specificities, and despite its high inherent susceptibility to reducing and denaturing agents, it is very stable upon immobilization and withstands even high concentration of guanidine hydrochloride and reducing agents. We show that denaturing agents can alter digestion by reducing protease activity and/or substrate solubility, and additionally, they influence the trapping of proteolytic peptides onto the reversed phase resin. Hydrogen/deuterium exchange coupled to mass spectrometry (HXMS) utilizes enzymatic digestion of proteins to localize the information about altered exchange patterns in protein structure. The ability of the protease to produce small peptides and overlapping fragments and provide sufficient coverage of the protein sequence is essential for localizing regions of interest. Recently, it was shown that there is an interesting group of proteolytic enzymes from carnivorous pitcher plants of the genus Nepenthes. In this report, we describe successful immobilization and the use of one of these enzymes, nepenthesin-1, in HXMS workflow. In contrast to pepsin, it has different cleavage specificities, and despite its high inherent susceptibility to reducing and denaturing agents, it is very stable upon immobilization and withstands even high concentration of guanidine hydrochloride and reducing agents. We show that denaturing agents can alter digestion by reducing protease activity and/or substrate solubility, and additionally, they influence the trapping of proteolytic peptides onto the reversed phase resin. (en)
Title	Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry (en)
skos:prefLabel	Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry (en)
skos:notation	RIV/00216208:11310/14:10282688!RIV15-MSM-11310___
http://linked.open...avai/riv/aktivita	I P S
http://linked.open...avai/riv/aktivity	I, P(EE2.3.30.0003), P(GAP206/12/0503), S
http://linked.open...iv/cisloPeriodika	9
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Man, Petr Kádek, Alan
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 / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	4180
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/14:10282688
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	fragmentation; rhizopuspepsin; dynamics; immobilization; proteins; h/d exchange; porcine pepsin; residue resolution; amide hydrogen-exchange; electron-transfer dissociation (en)
http://linked.open.../riv/klicoveSlovo	dynamics proteins fragmentation immobilization amide hydrogen-exchange electron-transfer dissociation h/d exchange porcine pepsin residue resolution rhizopuspepsin
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[67D328759DCE]
http://linked.open...i/riv/nazevZdroje	Analytical Chemistry
http://linked.open...in/vavai/riv/obor	CB
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	IMPULS, Inovation in Microbiology - Postdoctoral training and laboratory center Study of structure-function relationship in cellobiose dehydrogenase - a promising enzyme for applications in biosensors and biofuel cells
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	86
http://linked.open...iv/tvurceVysledku	Halada, Petr Man, Petr Mrázek, Hynek Kádek, Alan Rey, Martial Schriemer, David C.
http://linked.open...ain/vavai/riv/wos	000335719900033
issn	0003-2700
number of pages	8 (xsd:int)
http://bibframe.org/vocab/doi	10.1021/ac404076j
http://localhost/t...ganizacniJednotka	11310

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