What determines a protein's activity and capability?
Its 3D shape, which is the structure its 'string of amino acids' adopts.
What are the four levels of protein structure?
Primary, secondary, tertiary, and quaternary.
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Flashcards covering key concepts from the lecture notes on protein structure, including levels of structure, determining forces, secondary structures, tertiary structure, quaternary structure and protein denaturing.
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What determines a protein's activity and capability?
Its 3D shape, which is the structure its 'string of amino acids' adopts.
What are the four levels of protein structure?
Primary, secondary, tertiary, and quaternary.
What dictates the primary structure of a protein?
Covalent bonds between the amino acids.
What interactions determine the higher order structural features of proteins?
Non-covalent interactions.
What is the driving force that folds a protein into its 3D shape?
Hydrophobic interactions.
Where are charged residues typically located in a protein?
On the protein surface, interacting with water.
What type of covalent bond can form between two cysteine residues?
A disulfide bridge.
Where does all the information necessary to fold a protein into its unique 3D shape come from?
Its primary structure.
What property gives the amide bond some characteristics of a rigid, 'flat', double bond?
Its resonance properties.
What are the two common types of secondary structures in proteins?
Alpha-helix and beta-sheet.
What is the structure of alpha-helix?
A part of a single strand of amino acids coils itself into a helical shape.
How are alpha helices formed?
Through hydrogen bonds between peptide groups that are about 3.6 amino acids apart.
In beta-sheet, how are two or more segments of separate strands of amino acid aligned?
Side-by-side so that hydrogen bonds can form between peptide groups that are close to each other.
What are the names for the 3D shape of the entire protein?
Tertiary structure.
What are molecular chaperones also known as?
Heat shock proteins.
What is quaternary structure?
The assembly of multiple individual proteins into a single functional complex.
What type of interactions hold the individual components of quaternary structure together?
Weak, secondary interactions.
What happens during protein denaturing?
The disruption of the weak forces within the protein structure without breaking the covalent bonds.
Name methods that can cause Protein denaturing
Heating, changes in pH, adding organic solvents, adding salts, adding detergents, adding chaotropic agents