Relative stability of peptide sequence ions generated by tandem mass spectrometry. - Wikidata - wikimedia - TriplyDB

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

http://www.wikidata.org/entity/Q34165978

about

Insight into the Mechanism of Graphene Oxide Degradation via the Photo-Fenton Reaction CYCLONE--a utility for de novo sequencing of microbial cyclic peptides.Formation of a(1) ions directly from oxazolone b(2) ions: an energy-resolved and computational study.Comment on: "Quantum Chemical Mass Spectrometry: Verification and Extension of the Mobile Proton Model for Histidine" by Julie Cautereels and Frank Blockhuys, J. Am. Soc. Mass Spectrom. 28, 1227-1235 (2017).

P2860

Q28386229-7B0E25D8-D058-4B0C-8151-8F36761CC116 Q34736572-4CE92737-93B5-4612-9AD0-C0BB5029FFE5 Q41158494-5C0D3C86-7433-4D85-9FB2-988F99A2EC5D Q49796922-8CE8BD6D-698C-4243-A08D-89B98E3FD325

P2860

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

http://www.wikidata.org/entity/Q34165978

description

2012 nî lūn-bûn

@nan

2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@ast

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@en

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@nl

type

label

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@ast

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@en

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@nl

prefLabel

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@ast

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@en

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@nl

P1433

Q34165978-E64AD9F9-FECB-471D-91E8-72B7F10164A1

P1476

Q34165978-F7A00524-455A-4F0D-A0A4-D5D3CB4E625E

P2093

Q34165978-2E7D937E-FCA9-42AE-AD9A-D1984F8E4C16

Q34165978-44D37AC1-3FC3-48E2-AA88-A4A04DBAF4A5

Q34165978-5D493BA0-65CF-492D-A2A2-3B0DC35C1260

P2860

Q34165978-0177CEA7-BBA8-4F14-A210-A3DD62C9C269

Q34165978-0630C3E5-A81E-4C2D-BABD-F115C69600A3

Q34165978-09853DEA-4805-4641-AD7C-AD5DA8D2E6E2

Q34165978-19D6ECF3-2F9E-4203-B87A-851C978E83C4

Q34165978-1AE569A4-39C7-4B2F-AE42-86D3418A6475

Q34165978-1E6D4B56-AE62-4A7A-8069-09A1C34F2959

Q34165978-267CACE5-96A3-47EB-BF4D-D92D2E39BF33

Q34165978-26F7E12D-DADA-4E8B-858C-DC6195B132E7

Q34165978-28CC423A-4213-48A1-9A7C-DBD618978F04

Q34165978-2DACA240-514B-46F8-AFEB-CE4DB27FEF8F

P2888

Q34165978-E18222D9-F8B3-4351-A9ED-D995C931B4E8

P304

Q34165978-255FDDFB-546A-4AC2-B7E3-CC35C117A95C

P31

Q34165978-85FA16D9-8227-4933-9DC3-9CD0F53691C3

P356

Q34165978-FB021A1D-408B-43D9-904C-F0C5D2ACD907

P433

Q34165978-371077FA-B609-4890-8598-627F6F3CF4DC

P478

Q34165978-A5D62546-A1F1-45B4-8D7F-172670A21B5F

P577

Q34165978-294C78BE-1D2E-4EDC-94AA-2669AA6775AB

P5875

Q34165978-B32210D5-E546-4D0B-9FCD-3BA72258EA18

P6179

Q34165978-ABDA0254-3B2D-491F-BD4D-A5B1CDD53190

P698

Q34165978-A8460684-92C7-4FD4-8BE6-DCBE64FB865A

P356

S13361-012-0357-3

P1433

Journal of the American Society for Mass Spectrometry

P1476

Relative stability of peptide sequence ions generated by tandem mass spectrometry.

@en

P2093

Alan G Marshall

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

Benjamin J Bythell

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

Christopher L Hendrickson

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

P2860

Blackbody infrared radiative dissociation of bradykinin and its analogues: energetics, dynamics, and evidence for salt-bridge structures in the gas phase.

Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process

Gas phase activation energy for unimolecular dissociation of biomolecular ions determined by focused RAdiation for gaseous multiphoton ENergy transfer (FRAGMENT)

Combined electron capture and infrared multiphoton dissociation for multistage MS/MS in a Fourier transform ion cyclotron resonance mass spectrometer.

Energetics from slow infrared multiphoton dissociation of biomolecules

Vibrational signatures of protonated, phosphorylated amino acids in the gas phase.

Structure of electron-capture dissociation fragments from charge-tagged peptides probed by tunable infrared multiple photon dissociation.

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

Electrically compensated Fourier transform ion cyclotron resonance cell for complex mixture mass analysis.

Mobile and localized protons: a framework for understanding peptide dissociation.

P2888

s13361-012-0357-3

P304

644-654

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

P31

scholarly article

P356

10.1007/S13361-012-0357-3

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

P433

4

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

P478

23

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

P577

2012-02-22T00:00:00Z

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

P5875

221851510

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

P6179

1003757357

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

P698

22354685

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