CH-103 Chap 19
Card Set Information
CH-103 Chap 19
Organic Chemistry Proteins Amino Acids Zwitterions Peptides
Amino Acids & Proteins
Structural Protein; function and example:
: Provide structural components.
Collagen is in tendons and cartilage.
Keratin is in hair, skin, wool and nails.
Contractile protein; function and example:
: Move muscles.
Myosin and actin contract muscle fibers.
Transport protein; function and example:
: carry essential substances throughout the body.
Hemoglobin transports oxygen.
Lipoproteins transport lipids.
Storage protein; function and example:
: Store nutrients.
Casein stores protein in milk. Ferritin stores iron in the spleen and liver.
Hormone proteins; function and example:
: Regulate body metabolism and nervous system.
Insulin regulates blood glucose level.
Growth hormone regulates body growth.
Enzyme protein; function and example:
: Catalyze biochemical reactions in the cells.
Sucrase catalyzes the hydrolysis of sucrose. Trypsin catalyzes the hydrolysis of proteins.
Protection protein; function and example:
: Recognize and destroy foreign substances.
Immunoglobins stimulate immune responses.
Every Amino acid has:
a central carbon atom bonded to an ammonium group.
a carboxylate group (--COO
a Hydrogen atom.
a side chain or R group.
Nonpolar amino acids contain:
alkyl or aromatic R groups
this makes them hydrophobic.
Polar amino acids contain:
polar R groups such as hydroxyl (--OH), thiol (--SH) and amide (--CONH
these are hydrophylic.
Acidic Amino acids contain:
R groups that have carboxylate (--COO
Basic amino acids contain:
R groups that have ammonium (--NH
Describe the functional groups found in all alpha-Amino acids:
all amino acids contain a carboxylate group and an ammonium group on the alpha chain.
The use of electrical current to separate proteins or other charged molecules:
The pH at which an amino acid exists as a zwitterion with a net charge of zero:
The combination of two or more amino acids joined by peptide bonds:
The amide bond in that joins the carboxylate group of one amino acid with the ammonium group in the next amino acid:
a protein sttructure in which tow or more protein subunits form an active protein.
The attraction between the ionized R groups of basic and acidic amino acids in the tertiary structure of a protein.
The specific sequence of the amino acids in a protein.
The formation of an alpha-helix, Beta-pleated sheet, or triple helix.
The folding of the secondary structure of a protein into a compact structure that is stabilized by the interactions of R groups such as ionic and disulfide bonds.
The protein structure found in collage consisting of three polypeptide chains woven together like a braid.
The dipolar form of an amino acid consisting of two oppositely charged ionic regions, --NH