Electron capture versus energetic dissociation of protein ions

被引：98

作者：

Kruger, NA ^{[1
]}

Zubarev, RA ^{[1
]}

Carpenter, BK ^{[1
]}

Kelleher, NL ^{[1
]}

Horn, DM ^{[1
]}

McLafferty, FW ^{[1
]}

机构：

[1] Cornell Univ, Baker Lab Chem, Ithaca, NY 14850 USA

来源：

INTERNATIONAL JOURNAL OF MASS SPECTROMETRY | 1999年 / 182卷

关键词：

electron capture dissociation; multiply charged gaseous cations; collisionally activated dissociation; protein sequencing;

D O I：

10.1016/S1387-3806(98)14260-4

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

The identity of neighboring amino acids has little influence on the dissociation of multiply protonated proteins by electron capture dissociation. As exceptions, no cleavage occurs on the N-terminal side of Pro, and little on either side of Cys, whereas the C-terminal side of Trp is heavily favored. The neighboring amino acids have a far greater effect on energetic dissociation, making the combined methods promising for the de novo sequencing of proteins. (C) 1999 Elsevier Science B.V.

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页码：1 / 5

页数：5

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