Unit 4 Test Two Flashcards
What is primary structure
Sequence of amino acids in a polypeptide chain
What is secondary structure
Hydrogen bonds are the hallmark in this type of structure
What is tertiary structure
Stabilized by non covalent interactions and disulfide bonds
What is quaternary structure
Subunits represent basic component
What is a peptide bond
Linkage between the amino group of one amino acid and the carboxyl group of another amino acid
What is alpha helix
Stabilized by H bonds between nearby amino acids (n+4) in a polypeptide chain
What is motif
Super secondary structures in proteins
Examples of helix breakers
Proline and glycine
What are strong helix formers
Alanine and leucine
What are some examples of beta turn formers
Proline and glycine
What is a native fold
3D fold to fulfill specific biological function
What are favorable interactions in proteins
Hydrophobic effect, h bonds, London dispersion, and electrostatic interactions
What linkages are in primary structure
Covalent
What linkages in secondary structure
H bonds
What linkages in tertiary structure
Covalent, h bonds, ionic, van der waals, hydrophobic
Linkages in quarternary structures
Same as tertiary
What causes the peptide bond
Resonance
What type of degradation uses phenyl isothiocyanate which labels N terminal amino acid
Edman degradation
What reagent is used in edman degradation
Phenyl isothiocyanate
Structure of globular proteins
Tertiary and quarternary
Solubility of globular proteins
Fully soluble
Functions of globular proteins
Dynamic
Examples of globular protein
Hgb, myoglobin, enzymes
Structure of fibrous proteins
Primary and secondary
Solubility of fibrous proteins
Insoluble