z-logo
open-access-imgOpen Access
Solvent-Free Mass Spectrometry for Hydrophobic Peptide Sequence Analysis and Protein Conformation Studies
Author(s) -
Sarah Trimpin,
Max L. Deinzer
Publication year - 2005
Publication title -
biotechniques
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.617
H-Index - 131
eISSN - 1940-9818
pISSN - 0736-6205
DOI - 10.2144/05396te01
Subject(s) - mass spectrometry , peptide , chemistry , sequence (biology) , peptide sequence , bottom up proteomics , chromatography , protein mass spectrometry , biochemistry , tandem mass spectrometry , gene
The breakthrough in soft ionization methods for biopolymers, electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) (1,2), revolutionized mass spectrometry (MS). As a result of these effective bioanalytical technologies, the entire field of proteomics changed, and the use of mass spectrometers for protein identification by accurate mass measurements or de novo sequencing of the corresponding proteolytic peptides is now universally accepted. Bioanalytical techniques ideally aim for a maximum degree of unbiased analytical information hence, simplification of these techniques can become both more efficient and often more reliable. Such is the case with a new approach in the use of MALDI-MS.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom