Sections
Protein Purification
Protein Extraction
Differential Centrifugation
Salting Out
Dialysis
Column Chromatography
Ion-Exchange Chromatography
Anion-Exchange Chromatography
Size Exclusion Chromatography
Affinity Chromatography
Specific Activity
HPLC
Spectrophotometry
Native Gel Electrophoresis
SDS-PAGE
SDS-PAGE Strategies
Isoelectric Focusing
2D-Electrophoresis
Diagonal Electrophoresis
Mass Spectrometry
Mass Spectrum
Tandem Mass Spectrometry
Peptide Mass Fingerprinting
Overview of Direct Protein Sequencing
Amino Acid Hydrolysis
FDNB
Chemical Cleavage of Bonds
Peptidases
Edman Degradation
Edman Degradation Sequenator and Sequencing Data Analysis
Edman Degradation Reaction Efficiency
Ordering Cleaved Fragments
Strategy for Ordering Cleaved Fragments
Indirect Protein Sequencing Via Geneomic Analyses

Concept #1: Mass Spectrometry of Peptides

Practice: Considering the mass of each residue (shown below) and the fact that not every peptide bond will break in mass spectrometry of a protein, answer the following questions.

A) If cleavage between two Gly residues does not occur, which amino acid would be identified in place of the two glycines? 

a. Gly.                               c. Asp.

b. Asn.                              d. Ser.


B) What amino acid would be identified if a bond between Ser and Val did not break?

a. Trp.                               c. Thr.

b. Tyr.                               d. Val.