Dissociation of different conformations of ubiquitin ions.
نویسندگان
چکیده
The fragmentation pathways of different conformations of three charge states of ubiquitin ions are examined using ion mobility/collisional activation/time-of-flight techniques. Mass spectra for fragments for different conformers of a single charge state appear to be identical (within the experimental reproducibility). These results are consistent with a mechanism in which different conformers of each charge state rearrange to similar dissociation transition states prior to fragment formation.
منابع مشابه
Transitions between Elongated Conformations of Ubiquitin [M+11H]<sup>11+</sup> Enhance Hydrogen/Deuterium Exchange
’ INTRODUCTION Since the development of electrospray ionization for mass spectrometry (MS), several MS-based approaches have been developed for characterizing structures of gas-phase protein ions. These can be categorized as either chemical or physicalmethods. Chemical methods include: ion ion and ion molecule reactions, detection of noncovalent adducts, 9 and monitoring of hydrogen/deuterium (...
متن کاملGas-phase separations of protein and peptide ion fragments generated by collision-induced dissociation in an ion trap.
Ion mobility/time-of-flight mass spectrometry techniques have been used to examine distributions of fragment ions generated by collision-induced dissociation (CID) in a quadrupole ion trap. The mobility-based separation step prior to mass-to-charge (m/z) analysis reduces spectral congestion and provides information that complements m/z-based assignments of peaks. The approach is demonstrated by...
متن کاملPhotodissociation of conformer-selected ubiquitin ions reveals site-specific cis/trans isomerization of proline peptide bonds.
Ultraviolet photodissociation (UVPD) of gas-phase proteins has attracted increased attention in recent years. This growing interest is largely based on the fact that, in contrast to slow heating techniques such as collision induced dissociation (CID), the cleavage propensity after absorption of UV light is distributed over the entire protein sequence, which can lead to a very high sequence cove...
متن کاملConformational and noncovalent complexation changes in proteins during electrospray ionization.
Electrospray ion sources efficiently produce gas-phase ions from proteins and their noncovalent complexes. Charge-state distributions of these ions are increasingly used to gauge their conformations in the solution phase. Here we investigate how this correlation is affected by the spraying conditions at the early stage of droplet generation, prior to the ionization process. We followed the fold...
متن کاملInfluence of solvent composition and capillary temperature on the conformations of electrosprayed ions: unfolding of compact ubiquitin conformers from pseudonative and denatured solutions
High-resolution ion mobility/mass spectrometry methods have been used to examine the influence of solvent composition and capillary temperature on the gas-phase conformations of ubiquitin ions (16 to 113) formed during electrospray ionization. Three general conformer types are observed: compact forms (favored for the 16 and 17 charge states); partially folded conformers (favored for the 18 and ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of the American Society for Mass Spectrometry
دوره 13 6 شماره
صفحات -
تاریخ انتشار 2002