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Amino Acids

Key Properties and Structures of Proteins

TermDefinition
Proteins Polymers made from amino acids (aa).
Amino acids Building blocks of proteins, 20 types exist.
3D structure Determines protein function and activity.
Functional groups Chemical groups affecting amino acid properties.
Zwitterions Dipolar ions of amino acids at pH 7.
Chirality Amino acids exist in L and D forms.
L amino acids Only L forms are incorporated into proteins.
Alpha carbon Central carbon atom in amino acids.
R group Unique side chain defining each amino acid.
Ionization state Balance of protonated and deprotonated forms.
pH effect Affects amino acid charge and state.
Acidic solution pH 1, amino group protonated, carboxyl not dissociated.
Basic solution pH 9, amino group can donate protons.
Hydrophobic character Property of R groups affecting protein folding.
Hydrogen bonding capacity Ability of R groups to form hydrogen bonds.
Aliphatic R groups Hydrocarbon chains in amino acids.
Aromatic R groups Contain benzene rings in amino acids.
Polar R groups R groups with partial charges.
Basic R groups R groups that can accept protons.
Acidic R groups R groups that can donate protons.
Hydroxyl groups R groups containing -OH functional groups.
Amino acid nomenclature Unique names and codes for each amino acid.
R group Variable side chain of an amino acid.
Aromatic amino acids Amino acids with light-absorbing R groups.
Peptide bond Link between amino acids, releasing water.
Primary structure Sequence of amino acids in a protein.
Polypeptide chain Chain of amino acids linked by peptide bonds.
N-terminus Free amino group end of a polypeptide.
C-terminus Free carboxyl group end of a polypeptide.
Disulphide bond Covalent bond between two cysteine residues.
Secondary structure Folding patterns of polypeptide chains.
Alpha Helix Coiled structure in protein secondary structure.
Beta-pleated sheet Folded structure in protein secondary structure.
Trans configuration Most common peptide bond arrangement, stable.
Cis configuration Less common peptide bond arrangement, less stable.
Polarity of polypeptide Directionality from N-terminus to C-terminus.
Peptide bond stability Peptide bonds are stable and planar.
Protein length Proteins are typically 50-2000 amino acids long.
Peptides Short chains of amino acids, less than 50.
Energy requirement Energy is needed to form peptide bonds.
Planar peptide bond Peptide bonds restrict rotation around C atom.
Amino acid composition Backbone consists of C, H, and N atoms.
Protein function Determined by primary and secondary structures.
Secondary structure Includes α-helices and β-pleated sheets.
α-helix Rod-like structure with side chains outward.
Hydrogen bonds Stabilize α-helices between CO and NH groups.
Right-handed helix Most common helix type, less steric hindrance.
Ferritin Protein for iron storage, contains α-helices.
β-pleated sheet Strands almost fully extended, linked by hydrogen bonds.
Anti-parallel strands Strands run in opposite directions.
Parallel strands Strands run in the same direction.
Fatty acid binding protein Rich in β-sheets, contains one α-helix.
Tertiary structure Final 3D arrangement of a single protein.
Hydrophilic amino acids Dominant in linear proteins, face outward.
Hydrophobic residues Found inside globular proteins, such as valine.
Myoglobin Example protein illustrating tertiary structure.
Quaternary structure Formed by multiple tertiary proteins as subunits.
Hemoglobin Tetramer with two α and two β chains.
Created by: tunbridgeerin
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