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

Peptide Mass Fingerprinting

Biochemistry

5. Protein Techniques

Peptide Mass Fingerprinting

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Multiple Choice

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?

Carbon-carbon bonds within the amino acid R-groups.

Disulfide bonds.

Omega bonds.

Phi bonds.

Psi bonds.

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Verified step by step guidance

Understand the structure of a peptide: Peptides are composed of amino acids linked by peptide bonds, which are amide bonds between the carboxyl group of one amino acid and the amino group of another.

Identify the types of bonds in a peptide: In addition to peptide bonds, peptides have other types of bonds such as disulfide bonds (between cysteine residues), and bonds within the amino acid side chains (R-groups).

Recognize the role of tandem mass spectrometry in PMF: Tandem mass spectrometry is used to fragment peptides into smaller pieces, which helps in determining the sequence of the peptide by analyzing the mass-to-charge ratio of the fragments.

Determine which bonds are typically broken during fragmentation: In mass spectrometry, the peptide backbone is often cleaved at specific points, typically breaking the peptide bonds (also known as omega bonds) to generate a series of ions that can be analyzed.

Clarify the types of bonds mentioned: Omega bonds refer to the peptide bonds that are cleaved during fragmentation. Phi and psi bonds are related to the angles of rotation around the bonds in the peptide backbone, not typically broken in mass spectrometry. Disulfide bonds are covalent bonds that can be reduced but are not the primary focus in peptide fragmentation for PMF.