- Beta-sheets, providing flexibility.
- Alpha-helices, contributing to its strength and elasticity.
- Disulfide bridges, enhancing rigidity.
- Random coils, allowing for movement.
Category: Chemistry
- Molecular weight.
- Amino acid composition (number of each type of amino acid).
- Unique three-dimensional conformation.
- Solubility in water.
- Renaturation.
- Hydrolysis.
- Denaturation.
- Polymerization.
- Are composed of a single polypeptide chain folded into a complex shape.
- Exhibit extensive alpha-helix formation.
- Consist of two or more polypeptide subunits interacting to form a functional complex.
- Have a unique amino acid sequence.
- The protein's overall size and weight.
- The types of bonds formed in the secondary and tertiary structures, thus determining its final shape and function.
- The rate at which the protein can be synthesized.
- The protein's solubility in nonpolar solvents.
- Primary structure by breaking peptide bonds.
- Amino acid sequence.
- Secondary, tertiary, and sometimes quaternary structures by breaking weak bonds.
- Covalent bonds within the R-groups.
- Adjacent amino acids in the sequence.
- The carbonyl oxygen and amide hydrogen atoms of the backbone.
- The R-groups (side chains) of amino acids.
- Different polypeptide subunits.
- Parallel arrangement of polypeptide strands.
- A coiled shape maintained by hydrogen bonds running perpendicular to the helix axis.
- An extended zig-zag conformation.
- A coiled shape maintained by hydrogen bonds running parallel to the helix axis.
- Covalent bonds between R-groups.
- Hydrophobic interactions between nonpolar amino acids.
- Hydrogen bonds between the carbonyl oxygen and amide hydrogen of the polypeptide backbone.
- Ionic bonds between charged R-groups.
- Hydrogen bonds.
- Disulfide bonds.
- Peptide bonds.
- Ionic bonds.
- Three-dimensional folding pattern of a polypeptide chain.
- Specific sequence of amino acids in a polypeptide chain.
- Arrangement of multiple polypeptide subunits.
- Localized regions of alpha-helices and beta-sheets.
- Oligopeptides.
- Polypeptides.
- Amino acids.
- Dipeptides.
- Collagen.
- Keratin.
- Hemoglobin.
- Insulin.
- Fully functional enzymes.
- Randomly coiled structures.
- Intermediate products during protein breakdown or modification.
- Involved in genetic information storage.
- Peptide bond.
- Disulfide bridge.
- Prosthetic group.
- Alpha helix.
- Conjugated protein.
- Derived protein.
- Simple protein.
- Fibrous protein.
- Amino acids only.
- Amino acids and a non-protein prosthetic group.
- Sugars and amino acids.
- Fatty acids and glycerol.
- Glucose units.
- Fatty acids.
- Nucleotides.
- Amino acids.
