Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

5. Protein Techniques

Diagonal Electrophoresis

Biochemistry

5. Protein Techniques

Diagonal Electrophoresis

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Which of the following techniques is used specifically to help determine the site of a disulfide bond?

Edman degradation.

Affinity chromatography.

SDS-PAGE.

Diagonal electrophoresis.

MALDI-TOF Mass spectrometry.

Previous problemNext problem

Verified step by step guidance

Understand that disulfide bonds are covalent bonds formed between the sulfur atoms of two cysteine residues in a protein, which can affect the protein's structure and function.

Recognize that determining the site of a disulfide bond involves identifying which cysteine residues are linked by the bond.

Diagonal electrophoresis is a technique specifically designed to identify disulfide bonds by separating proteins based on their charge and size, and then breaking the disulfide bonds to observe changes in mobility.

In diagonal electrophoresis, proteins are first separated in one dimension, then treated with a reducing agent to break disulfide bonds, and finally separated in a second dimension. The shift in position indicates the presence and location of disulfide bonds.

Compare diagonal electrophoresis with other techniques: Edman degradation is used for sequencing amino acids, affinity chromatography for purifying proteins, SDS-PAGE for separating proteins by size, and MALDI-TOF mass spectrometry for determining molecular weights, none of which are specifically used to locate disulfide bonds.