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

Practice: Which advantage does native gel electrophoresis provide as a protein technique?

Practice: Which option below best describes the native gel electrophoresis migration for Proteins A, B, C & D (assuming equal mass & shape) considering that the buffer solution has a pH = 6.4. 

Protein A pI = 5.2, Protein B pI = 6.4, Protein C pI = 7.0, Protein D pI = 9.2

Practice: A) Consider both the peptide Gly—Pro—Ser—Glu—Thr (in a linear chain) and a cyclic peptide of the same exact sequence Gly—Pro—Ser—Glu—Thr (with a peptide bond linking the Thr & Gly). Are these peptides chemically the same? Explain.




B) Can you expect to separate the peptides above by Native-PAGE? Why or why not?