BIOL 4350 Lecture Notes - Lecture 9: Heat Shock Protein, Edman Degradation, N-Terminus

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9 Feb 2017
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FEBRUARY 6 PPT 5 (7-14) LECTURE 9
First 20 min=quiz
- QUIZ review (5/7 correct)
o Titration curve
Tyrosine proline (CORRECT)
o Generates ammonium as a product
Glutamate dehydrogenase (CORRECT)
o Isoelectric point of 6.5
PROLINE <3 (CORRECT)
o Crystals
4 (CORRECT)
o bonds
peptide and disulfide bonds are strong (not ionic bonds)
ionic bonds are the strongest of the weak interactions (INCORRECT)
o Polyubiquitin chain
Carboxyl terminus gets added to the amino terminus (INCORRECT)
o Heat shock proteins
Prevent interaction from unfolded and other unfolded proteins (CORRECT)
- Protein identification
o You can draw correlations between diseases and the nucleic acid content
o Proteomic correlationwhich proteins are more abundant than another
Analyze them by 2D SDS-PAGE and look for missing or overly abundant biomarker
o Protein sequencing
Edman degradation
Chemically modify the amino terminal residue that allows the residue to be
cleaved off of the protein
identify the amino acids step by step after the cleavage
most you can do is about 50 amino acids
o you blast the sequence and try and find the protein that contains those
50 amino acids
limitation is that you need a lot of protein
Mass spectrometry
Key thing is that you take proteins and break them up so that you can measure
their mass extremely accurately
You can deduce the sequence of the proteins
Requires that you ionize and evaporate your protein (make it gaseous)
2 different methods to do this
o matrix assisted laser desorption (MALDI-MS)
same time they get vaporized, they get ionized
o Electric spray ionization
Spray them through a super small capillary that separates the
proteins
Go into a flight tube and pulled into the detector at a rate the at corresponds to
their mass/charge ration (determine their mass(
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