期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 28, 期 7, 页码 1293-1303出版社
SPRINGER
DOI: 10.1007/s13361-016-1592-9
关键词
Metal coordinated peptide ions
资金
- Naval Surface Warfare Center, Crane Division by the Ph.D. Fellowship Program
- Naval Surface Warfare Center, Crane Division by the Naval Innovative Science and Engineering Program
- National Institute of Health [R01 GM103725]
- METACyt grant from the Lilly Endowment
Ion mobility mass spectrometry (IMS-MS) techniques were used to generate a database of 2288 collision cross sections of transition-metal-coordinated tryptic peptide ions. This database consists of cross sections for 1253 [Pep + X](2+) and 1035 [Pep + X + H](3+), where X2+ corresponds to Mn2+, Co2+, Ni2+, Cu2+, or Zn2+. This number of measurements enables the extraction of structural trends for transitionmetal- coordinated peptide ions. The range of structures and changes in collision cross sections for X2+-coordinated species (compared with protonated species of the same charge state) is similar to Mg2+-coordinated species. This suggests that the structures are largely determined by similarities in cation size with differences among the cross section distributions presumably caused by X2+ interactions with specific functional groups offered by the residue R-groups or the peptide backbone. Cross section contributions for individual residues upon X2+ solvation are assessed with the derivation of intrinsic size parameters (ISPs). The comparison of the [Pep + X](2+) ISPs with those previously reported for [Pep + Mg](2+) ions displays a lower contribution to the cross section for His, carboxyamidomethylated Cys, and Met, and is consistent with specific metal-residue interactions identified within protein X-ray crystallography databases.
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