Structural investigation of naturally occurring peptides by electron capture dissociation and AMBER force field modelling-Reference-Cited by-同舟云学术

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Structural investigation of naturally occurring peptides by electron capture dissociation and AMBER force field modelling

Published:2005-06-10 Issue:11-12 Volume:103 Page:1481-1489
ISSN:0026-8976
Container-title:Molecular Physics
language:en
Short-container-title:Molecular Physics

Author:

Polfer § Nick C.,Haselmann Kim F.,Langridge-Smith Pat R. R.,Barran * Perdita E.

Publisher

Informa UK Limited

Subject

Physical and Theoretical Chemistry,Condensed Matter Physics,Molecular Biology,Biophysics

Link

http://www.tandfonline.com/doi/pdf/10.1080/00268970500095998

Reference52 articles.

1. Protein Ladder Sequencing

2. Collisional effects on the charge distribution of ions from large molecules, formed by electrospray-ionization mass spectrometry

3. Surface-induced Dissociation: An Effective Tool to Probe Structure, Energetics and Fragmentation Mechanisms of Protonated Peptides

4. Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing

5. Tandem Mass Spectrometry of Large Biomolecule Ions by Blackbody Infrared Radiative Dissociation

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1. Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section;Chemical Reviews;2023-02-24

2. Characterization of native protein structure with ion mobility mass spectrometry, multiplexed fragmentation strategies and multivariant analysis;International Journal of Mass Spectrometry;2021-06

3. Recent Progress on Electron Capture Dissociation Mass Spectrometry;Acta Chimica Sinica;2019

4. Initial Protein Unfolding Events in Ubiquitin, Cytochrome c and Myoglobin Are Revealed with the Use of 213 nm UVPD Coupled to IM-MS;Journal of the American Society for Mass Spectrometry;2018-06-13

5. Use of Ultraviolet Photodissociation Coupled with Ion Mobility Mass Spectrometry To Determine Structure and Sequence from Drift Time Selected Peptides and Proteins;Analytical Chemistry;2016-10-03

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