MALDI-MS analysis of peptides modified with photolabile arylazido groups.
about
A matrix-assisted laser desorption/ionization compatible reagent for tagging tryptophan residues.Covalent attachment and dissociative loss of sinapinic acid to/from cysteine-containing proteins from bacterial cell lysates analyzed by MALDI-TOF-TOF mass spectrometry.Possible evidence of amide bond formation between sinapinic acid and lysine-containing bacterial proteins by matrix-assisted laser desorption/ionization (MALDI) at 355 nm.
P2860
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@ast
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@en
type
label
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@ast
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@en
prefLabel
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@ast
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@en
P2093
P2860
P1476
MALDI-MS analysis of peptides modified with photolabile arylazido groups.
@en
P2093
Dean Kirby
James Kang
Marilyn Perrin
William Low
Wolfgang H Fischer
P2860
P2888
P304
P356
10.1016/J.JASMS.2004.04.023
P577
2004-08-01T00:00:00Z
P5875
P6179
1042286838