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MCAT Bio. Chem Ch. 1
| Question | Answer |
|---|---|
| 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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