Podcast
Questions and Answers
Which type of secondary structure is stabilized by hydrogen bonds between carbonyl groups and NH groups on adjacent strands?
Which type of secondary structure is stabilized by hydrogen bonds between carbonyl groups and NH groups on adjacent strands?
- α-helix
- Random coil
- 310-helix
- β sheets (correct)
Which amino acids have high tendencies to form an α-helix?
Which amino acids have high tendencies to form an α-helix?
- Gly, Pro, His, Ile, Asn
- Phe, Tyr, Trp, Cys, Arg
- Glu, Asp, Val, Ser, Thr
- Ala, Leu, Lys, Met, uncharged Glu (correct)
In which type of secondary structure do neighboring side chains occupy opposite faces of the structure?
In which type of secondary structure do neighboring side chains occupy opposite faces of the structure?
- Random coil
- β sheets (correct)
- 310-helix
- α-helix
Which type of secondary structure is not frequently found in proteins?
Which type of secondary structure is not frequently found in proteins?
What is the distance between residues in the α-keratin α-helix?
What is the distance between residues in the α-keratin α-helix?
Which fibrous protein is mostly made up of β sheets?
Which fibrous protein is mostly made up of β sheets?
What defines the interface between two long helices in the coiled-coil structure typical of α-keratin?
What defines the interface between two long helices in the coiled-coil structure typical of α-keratin?
How many residues per turn does the α-helix have?
How many residues per turn does the α-helix have?
Which type of amino acid is Alanine?
Which type of amino acid is Alanine?
What type of conformation does Valine prefer?
What type of conformation does Valine prefer?
What is the meaning of 'amphiphilic' in the context of α‐helix and β‐strand?
What is the meaning of 'amphiphilic' in the context of α‐helix and β‐strand?
Why is the prediction of tertiary structure difficult?
Why is the prediction of tertiary structure difficult?
What is the primary reason for using a combination of approaches in protein amino acid sequence analysis?
What is the primary reason for using a combination of approaches in protein amino acid sequence analysis?
What is the initial form of insulin synthesis?
What is the initial form of insulin synthesis?
Study Notes
Secondary Structure
- β-sheet is stabilized by hydrogen bonds between carbonyl groups and NH groups on adjacent strands.
Amino Acids and Helices
- Amino acids with high tendencies to form an α-helix include alanine.
- Valine prefers a β-strand conformation.
Alpha-Keratin
- α-Keratin is a type of fibrous protein made up mostly of β sheets.
- The distance between residues in the α-keratin α-helix is 0.15 nm.
- The interface between two long helices in the coiled-coil structure of α-keratin is defined by ionic interactions between glutamic and lysine residues.
Structure Characteristics
- The α-helix has 3.6 residues per turn.
- α-Helix and β-strand are amphiphilic, meaning they have both hydrophilic and hydrophobic regions.
Protein Structure Analysis
- The prediction of tertiary structure is difficult due to the large number of possible conformations.
- A combination of approaches is used in protein amino acid sequence analysis to overcome the limitations of individual methods.
Insulin Synthesis
- The initial form of insulin synthesis is preproinsulin.
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Description
Test your knowledge of protein structure with this quiz covering topics like alpha-helix, beta-sheets, and the characteristics of amino acids. Identify the backbone components and R-groups, as well as the interactions between different regions and macromolecules.
