Chapter 8 Flashcards

1
Q

Know the structure of an amino acid

A

-amino group, carboxyl group, hydrogen, alpha carbon
-R groups differ in their chemical and physical properties

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2
Q

Know how amino acids are classified based on the structure and atomic makeup of their R group

A

-how they interact with water (hydrophobic/hydrophilic)
-whether they are basic or acidic
-whether they are polar or nonpolar

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3
Q

Compare hydrophobic and hydrophilic amino acids to one another

A

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

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4
Q

Know the three special amino acids and describe the effect these amino acids have on the proteins that incorporate them

A

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

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5
Q

Know the properties of peptide bond formation

A

-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

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6
Q

Know and compare the four levels of protein structure

A
  1. (Primary) = sequence of amino acids
  2. (Secondary) = interactions between stretches of nearby amino acids
    -alpha helix and beta sheet
  3. (Tertiary)= 3D shape of a protein
    -determines the protein’s function
  4. (Quaternary) = protein subunits interacting with one another
    -combination of subunits influence the function of the protein
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7
Q

Describe the processes of protein denaturation and renaturation

A

-denaturation= unfolding of proteins by chemical treatment or high temperatures; lose their function
-renaturation= refolding of protein in optimal conditions; regain function

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8
Q

Know the functional role of chaperone proteins in the folding of polypeptides

A
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