Chapter 8 Flashcards
(8 cards)
Know the structure of an amino acid
-amino group, carboxyl group, hydrogen, alpha carbon
-R groups differ in their chemical and physical properties
Know how amino acids are classified based on the structure and atomic makeup of their R group
-how they interact with water (hydrophobic/hydrophilic)
-whether they are basic or acidic
-whether they are polar or nonpolar
Compare hydrophobic and hydrophilic amino acids to one another
hydrophobic: located in the interior of folded proteins in order to be kept away from water
hydrophilic:
-polar side chains: hydrophilic and tend to form hydrogen bonds with one another or with water molecules
-basic and acidic amino acids are strongly polar and hydrophilic
-basic: positively charged
-acidic: negatively charged
-charged groups can form IONIC bonds with one another and with other charged molecules
Know the three special amino acids and describe the effect these amino acids have on the proteins that incorporate them
GLYCINE
-R group is hydrogen (symmetric)
-Nonpolar & small… the hydrogen side chain allows for freer rotation around the C-N bond
-effect=increases flexibility of the polypeptide backbone
PROLINE
-R group is linked back to the amino group
-effect:
-restricts rotation of the C-N bond
-puts constraints on the protein folding in the proline’s vicinity
CYETEINE:
-contains a -SH (sulfhydryl) group
-2 cysteines together can form S-S disulfide bonds: bridges that can connect different parts of the same protein or different proteins
Know the properties of peptide bond formation
-carboxyl group of one amino acid reacts with the amino group of another amino acid
-releases a water molecule
-the C=O group in the peptide bond is a carbonyl group & the N-H is an amide group
-the free amino group is at the amino end of the peptide & the carboxyl group is at the carboxyl end
-polymer of amino acids connected by polypeptide bonds is a polypeptide
Know and compare the four levels of protein structure
- (Primary) = sequence of amino acids
- (Secondary) = interactions between stretches of nearby amino acids
-alpha helix and beta sheet - (Tertiary)= 3D shape of a protein
-determines the protein’s function - (Quaternary) = protein subunits interacting with one another
-combination of subunits influence the function of the protein
Describe the processes of protein denaturation and renaturation
-denaturation= unfolding of proteins by chemical treatment or high temperatures; lose their function
-renaturation= refolding of protein in optimal conditions; regain function
Know the functional role of chaperone proteins in the folding of polypeptides