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: Peptide Mass Fingerprinting

Practice: Peptide mass fingerprinting (PMF) is a method used to determine the sequence of an unknown peptide. In the sequencing of peptides by PMF, tandem mass spectrometry fragments peptides into smaller molecules to obtain the mass spectrum, which acts like a fingerprint & can be compared to theoretical spectrums in a database to derive the amino acid sequence. Mainly which types of bonds are broken to fragment the peptide & generate tandem mass spectra data?

Practice: Explain how a 5-residue amino acid sequence could uniquely identify a 200-residue protein via PMF. 

Hint #1: Compare the number of pentapeptides in the 200-residue protein to the total number of all possible pentapeptide sequences.

Hint #2: 

Hint #3: