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

4. Protein Structure

Tertiary Structure of Protein

Biochemistry

4. Protein Structure

Tertiary Structure of Protein

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Multiple Choice

Which of the following is true regarding the tertiary structure of G3P dehydrogenase?

Its tertiary structure involves its entire 2D-structure.

Its tertiary structure is primarily stabilized by peptide backbone interactions.

Its R-group interactions stabilize its tertiary structure.

Only R-groups that are nearby in its primary sequence can interact.

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Verified step by step guidance

Understand the concept of tertiary structure in proteins: Tertiary structure refers to the three-dimensional folding of a protein molecule, which is stabilized by interactions between the side chains (R-groups) of the amino acids.

Analyze the image of G3P dehydrogenase: The image shows a complex 3D structure, indicating the presence of multiple interactions that contribute to the protein's tertiary structure.

Identify the types of interactions that stabilize tertiary structure: These include hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, all of which occur between R-groups of amino acids.

Evaluate the statement about peptide backbone interactions: While peptide backbone interactions are important for secondary structure (alpha helices and beta sheets), tertiary structure is primarily stabilized by R-group interactions.

Consider the proximity of R-groups in primary sequence: Tertiary structure allows for interactions between R-groups that are not necessarily adjacent in the primary sequence, as the protein folds into its functional 3D shape.