Biochemistry - Proteins
10 important questions on Biochemistry - Proteins
Structure of amino acid (Fischer projection)
Amino group
Carboxyl group
R - group
H
Acid Base characteristics of an amino acid
- Each site is fully protonated, Amine group in NH3+, Carboxyl group is OH
Neutral solution:
- Exists as a zwitterion, Amine group is NH3+, Carboxyl group is OH-
Basic Solution:
- Each site is fully deprotonated, Amine group is NH2, Carboxyl group is OH-
Dissociation constant of amino acids
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Titration curve of an AA
AA acts as a buffer around the dissociation points
2 moles of base added / 1 mole of AA ( 2 dissociation points)
Can titrate in reverse
Polar Amino Acids
Found on the surface of proteins, as are hydrophilic
- Methionine
- Threonine
- Serine
- Cysteine
- Tyrosine
- Asparagine
- Glutamine
Acidic Amino Acids
Extra COOH group gives the molecule a third dissociation constant, the PI is closer to more acidic PKa (PKa1, PI, PKa2, PKa3)
Takes 3 moles base to titrate 1 mole AA
Aspartate (Aspartic acid)
Glutamate (Glutamic acid)
Resonance of peptide chains
Secondary protein structure
alpa helix - coils clockwise, stabilized by intramolecular H bonds between every 4 A.A.s. Side chains point away from core
Beta pleated sheets - chains lie next to each other in rows, form a sheet. held together by H bonds. Assumes a rippled shape due to the number of H bonds present. R groups point above and below the plane.
Tertiary protein structure
Fibrous protein: found in sheets or long strands
Globular protein: spherical in shape
Quaternary protein structure
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