Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling. - Wikidata - wikimedia - TriplyDB

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

http://www.wikidata.org/entity/Q37734636

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Application of GC/MS Soft Ionization for Isomeric Biological Compound Analysis.Peptide scrambling during collision-induced dissociation is influenced by N-terminal residue basicity

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Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

http://www.wikidata.org/entity/Q37734636

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article científic

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article scientifique

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articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 17 December 2013

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vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

@en

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

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label

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

@en

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

@nl

prefLabel

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

@en

Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling.

@nl

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Analytical Chemistry

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Gas-phase ion isomer analysis reveals the mechanism of peptide sequence scrambling

@en

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Chenxi Jia

http://www.w3.org/2001/XMLSchema#string

Christopher B Lietz

http://www.w3.org/2001/XMLSchema#string

Lingjun Li

http://www.w3.org/2001/XMLSchema#string

Qiang Cui

http://www.w3.org/2001/XMLSchema#string

Zhidan Liang

http://www.w3.org/2001/XMLSchema#string

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Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry.

CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields

All-atom empirical potential for molecular modeling and dynamics studies of proteins

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Mass spectrometry of peptides and proteins

Fragmentation reactions of multiply-protonated peptides and implications for sequencing by tandem mass spectrometry with low-energy collision-induced dissociation

To b or not to b: the ongoing saga of peptide b ions.

Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites.

Molecular dynamics and ion mobility spectrometry study of model β-hairpin peptide, trpzip1.

Number of solution states of bradykinin from ion mobility and mass spectrometry measurements.

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2917-2924

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scholarly article

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10.1021/AC401578P

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6

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86

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2013-12-17T00:00:00Z

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259209808

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24313304

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