Publication Date:
2006-10-07
Description:
For characterization of sequence and posttranslational modifications, molecular and fragment ion mass data from ionizing and dissociating a protein in the mass spectrometer are far more specific than are masses of peptides from the protein's digestion. We extend the approximately 500-residue, approximately 50-kilodalton (kD) dissociation limitation of this top-down methodology by using electrospray additives, heated vaporization, and separate noncovalent and covalent bond dissociation. This process can cleave 287 interresidue bonds in the termini of a 1314-residue (144-kD) protein, specify previously unidentified disulfide bonds between 8 of 27 cysteines in a 1714-residue (200-kD) protein, and correct sequence predictions in two proteins, one with 2153 residues (229 kD).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, Xuemei -- Jin, Mi -- Breuker, Kathrin -- McLafferty, Fred W -- GM16609/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):109-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023655" target="_blank"〉PubMed〈/a〉
Keywords:
Acyltransferases/chemistry
;
Amino Acid Sequence
;
Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor/chemistry
;
Chemistry, Physical
;
Complement C4/chemistry
;
Cysteine/chemistry
;
Humans
;
Mass Spectrometry/*methods
;
Molecular Weight
;
Peptide Fragments/chemistry
;
Physicochemical Phenomena
;
Protein Conformation
;
Protein Folding
;
Protein Processing, Post-Translational
;
Proteins/*chemistry
;
Proteomics
;
Spectrometry, Mass, Electrospray Ionization/*methods
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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