Indiana Section of the Society for Applied SpectroscopyIndiana Section of the Society for Applied Spectroscopy
1999-2000 Seminar Abstracts
TWO DIMENSIONAL MASS SPECTROMETRY OF BIOMOLECULES:
FLIP
YOUR IONS THE “BIRD”
Dr.
Evan R. Williams
Department
of Chemistry, University of California, Berkeley, CA
94720
williams@cchem.berkeley.edu
The application of mass spectrometry to the
structural characterization of large biopolymers has undergone explosive growth
in the last several years. Mass
spectrometry can provide molecular weights of large proteins and DNA with
unprecedented accuracy (± 1-3 Da at 100,000 Da) and sensitivity (sub-attomole
detection possible). In addition to
accurate molecular weights, information about sequence, locations of
posttranslational modifications and binding sites can be obtained using
two-dimensional mass spectrometry or tandem MS. One method for this, blackbody infrared radiative
dissociation or BIRD, can provide accurate information about the dissociation
energies and mechanisms for large ions. The
structure and energetics of a wide variety of biomolecule ions, including
oligonucleotides, peptides, and proteins have been investigated with BIRD.
These experiments indicate that conformation plays a significant role in
the gas-phase ion chemistry as it does in solution.
In addition, many aspects of solution-phase structure are preserved in
the complete absence of solvent, including zwitterions, salt bridges, and
Watson-Crick base pairing in DNA duplexes.
Gas-phase ions of large biomolecules can also be produced with a
sufficient number of water molecules attached such that they should have
solution-phase structures. These
results suggest that mass spectrometry can provide a bridge between the pure
gas-phase structure of an isolated biomolecule and the chemistry of the
biomolecule in aqueous solution.
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