|
Volumn 267, Issue 1, 1999, Pages 169-184
|
Spontaneous α-N-6-phosphogluconoylation of a 'His tag' in Escherichia coli: The cause of extra mass of 258 or 178 Da in fusion proteins
|
Author keywords
[No Author keywords available]
|
Indexed keywords
ACYLATION;
ESCHERICHIA COLI;
GLUCOSE;
MASS SPECTROMETRY;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
DEPHOSPHORYLATIONS;
GLUCOSE-6-PHOSPHATE DEHYDROGENASE;
HIS-TAGGED PROTEINS;
MODIFIED PROTEINS;
PERIODATE OXIDATION;
PLAUSIBLE MECHANISMS;
POST-TRANSLATIONAL MODIFICATIONS;
TANDEM MASS SPECTROMETRY;
PROTEINS;
6 PHOSPHOGLUCONOYL 1,5 LACTONE;
GLUCOSE 6 PHOSPHATE DEHYDROGENASE;
HISTIDINE;
HYBRID PROTEIN;
UNCLASSIFIED DRUG;
ACYLATION;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING KINETICS;
ESCHERICHIA COLI;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE IMAGING;
OXIDATION;
PEPTIDE SYNTHESIS;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN EXPRESSION;
PROTEIN MODIFICATION;
PROTEIN STRUCTURE;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
|
EID: 0033080755
PISSN: 00032697
EISSN: None
Source Type: Journal
DOI: 10.1006/abio.1998.2990 Document Type: Article |
Times cited : (175)
|
References (19)
|