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Again, state the 5 properties of proteins that can be exploited.
Mass
Charge-pH
Hydrophobic/hydrophilic interactions
Differential solubility
Mobility in applied fields
Define the effect of a kosmotropic molecule.
Contribute to structure and stability of water-water interactions, stabalising intermolecular inetarctions in proteins
Define the effect of a chaotropic molecule.
Disrupt water-water interactions, increasing the solubility of non-polar molecules
In N-terminal sequencing, what is added to remove the outermost amino acid?
A mildly basic buffer is also added, state the name of this buffer.
Phenyl IsoThioCyanate (PITC)
Trimethylamine
In N-teminal sequencing, what is used to allow the terminal amino acid to be selectively removed?
This derivative then isomerises to give a substituted_?
What process allows this^ to be identified?
Anhydrous acid
Phenylthiohydantoin
Chromatography
Often the N-teminal amino acid is chemically modified. How is this modification enzymatically removed?
State a limitation of the Edman degradation.
Pyroglutamylcarboxyl peptidase
Answer can include:
Cannot determine the position of disulfide bonds
or only a linear sequence of amino acids produced
In mass spectronomy protein sequencing, peptides are produced using specific proteases and cyanogen bromide. How are these peptides fractionated?
High Performance Liquid Chromatography (HPLC)
The peptides are run through the MS twice.
What happens during run 1?
What happens during run 2?
1: Mass of peptide is determined
2: Peptide is fragmented and different mass of the individual amino acids is determined
Runs 1 and 2 can now be done in 1 single step, know as?
What happens once the data on m/z ratio has been discovered?
Tandem Mass Spectronomy
Compared against a database of previously sequenced proteins in order to determine the sequences of the fragments
In CID mass spectronomy, what does CID stand for?
Collision Induced Dissociation
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