Ch. 4 - Protein StructureWorksheetSee all chapters
All Chapters
Ch. 1 - Introduction to Biochemistry
Ch. 2 - Water
Ch. 3 - Amino Acids
Ch. 4 - Protein Structure
Ch. 5 - Protein Techniques
Ch. 6 - Enzymes and Enzyme Kinetics
Ch. 7 - Enzyme Inhibition and Regulation
Ch. 8 - Protein Function
Ch. 9 - Carbohydrates
Ch. 10 - Lipids
Ch. 11 - Biological Membranes and Transport
Ch. 12 - Biosignaling
Clutch Review 1: Nucleic Acids, Lipids, & Membranes
Clutch Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway
Clutch Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism
Clutch Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation
Sections
Peptide Bond
Primary Structure of Protein
Altering Primary Protein Structure
Drawing a Peptide
Determining Net Charge of a Peptide
Isoelectric Point of a Peptide
Approximating Protein Mass
Peptide Group
Ramachandran Plot
Atypical Ramachandran Plots
Alpha Helix
Alpha Helix Pitch and Rise
Alpha Helix Hydrogen Bonding
Alpha Helix Disruption
Beta Strand
Beta Sheet
Antiparallel and Parallel Beta Sheets
Beta Turns
Tertiary Structure of Protein
Protein Motifs and Domains
Denaturation
Anfinsen Experiment
Protein Folding
Chaperone Proteins
Quaternary Structure
Simple Vs. Conjugated Proteins
Fibrous and Globular Proteins

Concept #1: Factors that Disrupt Alpha Helix Structure

Practice: Why does poly-L-Glutamate adopt an α-helical structure at low pH but a random conformation above pH 5?

Concept #2: Gly and Pro Disrupt Alpha Helices

Practice: Which of the following peptides is more likely to take up an α-helical structure and why?

Practice: An α-helix would be destabilized most by:

Practice: At pH 6.8, which of the following peptides is least likely to form an α-helix?

Peptide # 1: RSEDNFGAPKSILWE                    Peptide # 2: DQKASVEMAVRNSGK

Practice: Why does proline often “break” an alpha helix?