Abstract
Three synthetic peptides, derived from the human potassium channel proteins Ether-a-go-go-related gene (HERG), KCNQ1, and KCNE1, were investigated by hydrogen deuterium exchange coupled with electrontransfer dissociation mass spectrometry at single residue resolution. Each amino acid residue in the first half of the HERG peptide incorporated deuterons with a higher rate than those in the second half of the peptide, consistent with the nuclear magnetic resonance structure of this peptide, with amino acids 1-10 being a flexible coil, whereas amino acids 11-24 are a stable amphipathic helix. The binding interface of KCNQ1 and KCNE1 was determined by comparing the difference of sequential fragment ions before and after binding. The residues determined to be involved in bindingwere consistentwith a cysteine cross-linking study and confirmed by double mutant cycle analysis.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1303-1309 |
| Number of pages | 7 |
| Journal | Analytical and Bioanalytical Chemistry |
| Volume | 403 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2012 |
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Keywords
- C-Type fragment ions
- Deuterium incorporation
- Electron-transfer dissociation mass spectrometry
- Hydrogen deuterium exchange (HDX)
- Hydrogenscrambling
- Z-Type fragment ions
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
Cite this
Binding interface of cardiac potassium channel proteins identified by hydrogen deuterium exchange of synthetic peptides. / Chen, Jerri; Angeletti, Ruth; McDonald, Thomas V.; Xiao, Hui.
In: Analytical and Bioanalytical Chemistry, Vol. 403, No. 5, 05.2012, p. 1303-1309.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding interface of cardiac potassium channel proteins identified by hydrogen deuterium exchange of synthetic peptides
AU - Chen, Jerri
AU - Angeletti, Ruth
AU - McDonald, Thomas V.
AU - Xiao, Hui
PY - 2012/5
Y1 - 2012/5
N2 - Three synthetic peptides, derived from the human potassium channel proteins Ether-a-go-go-related gene (HERG), KCNQ1, and KCNE1, were investigated by hydrogen deuterium exchange coupled with electrontransfer dissociation mass spectrometry at single residue resolution. Each amino acid residue in the first half of the HERG peptide incorporated deuterons with a higher rate than those in the second half of the peptide, consistent with the nuclear magnetic resonance structure of this peptide, with amino acids 1-10 being a flexible coil, whereas amino acids 11-24 are a stable amphipathic helix. The binding interface of KCNQ1 and KCNE1 was determined by comparing the difference of sequential fragment ions before and after binding. The residues determined to be involved in bindingwere consistentwith a cysteine cross-linking study and confirmed by double mutant cycle analysis.
AB - Three synthetic peptides, derived from the human potassium channel proteins Ether-a-go-go-related gene (HERG), KCNQ1, and KCNE1, were investigated by hydrogen deuterium exchange coupled with electrontransfer dissociation mass spectrometry at single residue resolution. Each amino acid residue in the first half of the HERG peptide incorporated deuterons with a higher rate than those in the second half of the peptide, consistent with the nuclear magnetic resonance structure of this peptide, with amino acids 1-10 being a flexible coil, whereas amino acids 11-24 are a stable amphipathic helix. The binding interface of KCNQ1 and KCNE1 was determined by comparing the difference of sequential fragment ions before and after binding. The residues determined to be involved in bindingwere consistentwith a cysteine cross-linking study and confirmed by double mutant cycle analysis.
KW - C-Type fragment ions
KW - Deuterium incorporation
KW - Electron-transfer dissociation mass spectrometry
KW - Hydrogen deuterium exchange (HDX)
KW - Hydrogenscrambling
KW - Z-Type fragment ions
UR - http://www.scopus.com/inward/record.url?scp=84862816552&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84862816552&partnerID=8YFLogxK
U2 - 10.1007/s00216-012-5857-2
DO - 10.1007/s00216-012-5857-2
M3 - Article
C2 - 22392372
AN - SCOPUS:84862816552
VL - 403
SP - 1303
EP - 1309
JO - Fresenius Zeitschrift fur Analytische Chemie
JF - Fresenius Zeitschrift fur Analytische Chemie
SN - 0016-1152
IS - 5
ER -