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MCAT Bio. Chem Ch. 1

Amino Acids Have 4 groups attached to a central (alpha) carbon including: an amino group, a carboxylic acid group, an H-atom, and an R group
R Group Determines chemistry and function of an amino acid
Amount of Amino Acids That Appear In Proteins Of Eukaryotic Organisms 20
Stereochemistry Of The Alpha-Carbon For All Amino Acids In Eukaryotes L
Note About D-Amino Acids They can exist in prokaryotes
All Amino Acids Except Cysteine Has This Config: S config.
All Amino Acids Except Glycine Are: Chiral
Glycine Has a hydrogen atom as its R group
Charge Properties Of Side Chains They can be polar or nonpolar, aromatic or nonaromatic, charged or uncharged
Nonpolar, Nonaromatic Amino Acids Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline
Aromatic Amino Acids Tryptophan, Phenylalanine, Tyrosine
Polar Amino Acids Serine, Threonine, Asparagine, Glutamine, Cysteine
Negatively Charged (Acidic) Amino Acids Aspartate, Glutamate
Positively Charged (Basic) Lysine, Arginine, Histidine
Hydrophobicity Of Amino Acids With Long Alkyl Chains Hydrophobic
Hydrophobicity Of Amino Acids With Charges Hydrophillic
Amphoteric Ability of an amino acid to accept or donate protons
pKa Of An Amino Acid Group pH at which half of the species is deprotonated. [HA] = [A-]
Amino Acids At Low (Acidic) pH Values Amino acid is fully protonated
Amino Acids Near pI Of Amino Acid Become a neutral zwitterion
Amino Acids At High (Alkaline) pH Values Amino acid is fully deprotonated
How The Isoelectric Point (pI) Of An Amino Acid Without A Charged Side Chain Can Be Calculated Average the two pKa values.
Can Amino Acids Be Titrated? Yes
Titration Curve At The pKa Values Of An Amino Acid Nearly flat
Titration Curve At The pI Of An Amino Acid Nearly vertical
Can Amino Acids With Charged Side Chains Have An Additional pKa value? Yes
How To Calculate The pI Of An Amino Acid Average the two pKa values that correspond to protonation and deprotonation of the zwitterion
Gen. pI Of Amino Acids Without Charged Side Chains 6
Gen. pI Of Acidic Amino Acids Well below 6
Gen. pI Of Basic Amino Acids Well above 6
Dipeptides Have two amino acid residues
Tripeptides Have three amino acid residues
Oligopeptides Have a "few" amino acids (<20)
Polypeptides Have a "many" amino acids (>20)
Condensation / Dehydration Reaction Forms a peptide bond by a releasing 1 molecule of water
Nucleophilic Amino Group Of An Amino Acid Attacks the electrophilic carbonyl group of another amino acid.
Reason Why Amide Bonds Are Rigid Due to resonance
Hydrolysis Reaction Involves the breaking of a peptide bond.
Primary Structure Linear sequence of amino acids in a peptide and is stabilized by peptide bonds.
Secondary Structure Local structure of neighboring amino acids, and is stabilized by h-bonding between amino groups and nonadjacent carboxyl groups.
Alpha-Helices Clockwise coils around a central axis
Beta-Pleated Sheets Rippled strands that can be parallel or antiparallel
Proline Can interrupt secondary structure because of its rigid cyclic structure.
Tertiary Structure 3-D shape of a single polypeptide chain, and is stabilized by hydrophobic interactions, acid-base interactions (salt bridges), h-bonding, and disulfide bonds.
Hydrophobic Interactions Push hydrophobic R groups to the interior of a protein, which increases entropy of the surrounding water molecules and creates a negative Gibbs free energy.
Disulfide Bonds Occur when two cysteine molecules are oxidized and create a covalent bond to form cystine.
Quaternary Structure Interaction between peptides in proteins that contain multiple subunits.
Conjugated Proteins Proteins with covalently attached molecules
Prosthetic Group Attached molecule to a protein via a covalent bond, which could be a metal ion, vitamin, lipid, carbohydrate, or nucleic acid.
Denaturation Loss of 3-D protein structure due to heat and increasing solute concentration
Created by: SamB91
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