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Structural Protein; function and example:
- Function: Provide structural components.
- Collagen is in tendons and cartilage.
- Keratin is in hair, skin, wool and nails.
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Contractile protein; function and example:
- Function: Move muscles.
- Myosin and actin contract muscle fibers.
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Transport protein; function and example:
- Function: carry essential substances throughout the body.
- Hemoglobin transports oxygen.
- Lipoproteins transport lipids.
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Storage protein; function and example:
- Function: Store nutrients.
- Casein stores protein in milk. Ferritin stores iron in the spleen and liver.
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Hormone proteins; function and example:
- Function: Regulate body metabolism and nervous system.
- Insulin regulates blood glucose level.
- Growth hormone regulates body growth.
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Enzyme protein; function and example:
- Function: Catalyze biochemical reactions in the cells.
- Sucrase catalyzes the hydrolysis of sucrose. Trypsin catalyzes the hydrolysis of proteins.
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Protection protein; function and example:
- Function: Recognize and destroy foreign substances.
- Immunoglobins stimulate immune responses.
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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.
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Nonpolar amino acids contain:
- alkyl or aromatic R groups
- this makes them hydrophobic.
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Polar amino acids contain:
- Neutral
- polar R groups such as hydroxyl (--OH), thiol (--SH) and amide (--CONH2).
- these are hydrophylic.
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Acidic Amino acids contain:
R groups that have carboxylate (--COO-).
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Basic amino acids contain:
R groups that have ammonium (--NH3+).
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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.
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The use of electrical current to separate proteins or other charged molecules:
Electrophoresis.
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The pH at which an amino acid exists as a zwitterion with a net charge of zero:
isoelectric point.
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The combination of two or more amino acids joined by peptide bonds:
Peptide.
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The amide bond in that joins the carboxylate group of one amino acid with the ammonium group in the next amino acid:
Peptide bond.
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Quaternary structure:
a protein sttructure in which tow or more protein subunits form an active protein.
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Salt Bridge:
The attraction between the ionized R groups of basic and acidic amino acids in the tertiary structure of a protein.
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Primary structure:
The specific sequence of the amino acids in a protein.
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Secondary Structure:
The formation of an alpha-helix, Beta-pleated sheet, or triple helix.
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Tertiary structure:
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.
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Triple helix:
The protein structure found in collage consisting of three polypeptide chains woven together like a braid.
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Zwitterion:
The dipolar form of an amino acid consisting of two oppositely charged ionic regions, --NH3+ and --COO-.
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