CH908, Problem set 12 - Noncovalent complexes and protein
conformation.
1. Explain two methods for generating unfolding (melting) curves for
proteins using mass spectrometry. What kind of resolution can be
achieved?
2. What are some advantages of using mass spectrometry to study
protein structure rather than crystallography? Disadvantages?
3. labeling reactions, such as crosslinking, can be useful, but they
make for difficult MS/MS spectra. Why? As an example, consider the
fragments you'd expect if the following two peptides were crosslinked
from the aspartic acid on Peptide 1 to the central lysine on Peptide 2
(using a zero-length crosslinker).
Peptide 1: RGAVIVWYSDGK
Peptide 2: QQLMGPKGAVLK
Can you calculate the expected b/y fragments in this case?