Part II => PROTEINS and ENZYMES. 2.1 AMINO ACIDS 2.1a Nomenclature 2.1b Stereochemistry 2.1c Derivatives
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1 Part II => PROTEINS and ENZYMES 2.1 AMINO ACIDS 2.1a Nomenclature 2.1b Stereochemistry 2.1c Derivatives
2 Section 2.1a: Nomenclature
3 Synopsis 2.1a - Proteins (or polypeptides) are polymers made up of building blocks, or monomeric units, called amino acids - There are 20 naturally-occurring amino acids referred to as standard amino acids or -amino acids - Standard amino acids share a common structure but differ in their side chains the so-called R group - Amino acids are linked together to generate a polypeptide chain via so-called peptide or amide bonds - Some amino acid side chains harbor ionizable groups with distinct pk values
4 General Structure of -Amino Acids - Except for proline, all amino acids are constructed from a primary amino (-NH 2 ) group and a carboxylic acid (-COOH) group linked together via a carbon atom called C - For its part, proline harbors a secondary amino (-RNH) group and a carboxylic acid (-COOH) group Amino group Sidechain group Carboxylic Acid group - Amino acid nomenclature is based on a three-letter code and a one-letter code eg glycine (the simplest amino acid with R=H) can be denoted as Gly or G - The 20 standard amino acid residues can be sub-divided into three major categories depending on the chemical nature of their sidechain groups: (1) Apolar Residues (2) Polar Residues (3) Charged Residues
5 Amino Acids: (1) Apolar Residues Hydrogen Methyl Phenyl Pyrrolidine Isopropyl (iso: equal) Isobutyl (cf: sec-, tert-, and n-butyl) Benzene Pyrrole sec-butyl (sec: secondary) S-Methylethyl (thioether) Pyrrolidine Benzyl (phenyl) aromatic Indole Indolylmethyl (indole) aromatic
6 Amino Acids: (2) Polar Residues > 14 (hydroxyl) Hydroxymethyl (hydroxyl) > 14 (hydroxyl) Hydroxyethyl (hydroxyl) Amidomethyl (amide) Amidoethyl (amide) Hydroxybenzyl (hydroxyl) aromatic Sulfhydromethyl (sulfhydryl/thiol)
7 Amino Acids: (3) Charged Residues Aminobutyl (amine) Basic Residues Guanidinopropyl (guanidine) Imidazolylmethyl (imidazole) aromatic Basic or Neutral Acetate (carboxyl) Propionate (carboxyl) - In the context of globular proteins, the pk values of sidechain ionizable groups often differ from those stated above (for free amino acids) by as much as several units When ph < pk, R group is protonated and vice versa! - Such discrepancy arises due to electrostatic interactions of ionizable sidechain groups with other charged and/or apolar sidechains Guanidine Acidic Residues Imidazole
8 Amino Acid: Stick Model R H 2 N Stick model COOH - The stick model provides a neat way to understand the chemical structures of amino acids one just has to recall the chemical nature of the R group! - Only four amino acids (ie Trp, Phe, Tyr and His) harbor an aromatic R group - Aromaticity implies that the R group is a (hetero)cyclic ring with a conjugated ie alternating single C-C and double C=C bonds delocalized bond system
9 Dipolar Amino Acids: Zwitterions Sidechain (atoms) Backbone (atoms) - pk values of amino and carboxylic groups are respectively around 9 and 2 - Under physiological settings (ph 7-8), amino acids thus exist as charged dipolar ions - Such oppositely charged dipolar ions are referred to as zwitterions
10 Amino Acid Atom Nomenclature -amino -carboxyl - The various atoms along the sidechain R group are usually denoted by Greek alphabets starting with the central carbon (C ) atom linking the backbone amino and carboxylic groups which are respectively referred to as -amino and -carboxyl groups -amino -carboxyl - Accordingly, the sidechain functional groups such as those in Lys and Glu are respectively called -amino and -carboxyl groups so as to distinguish them from their backbone counterparts - By virtue of their backbone and sidechain functional groups, amino acids engage in TWO major inter-residue covalent linkages: (1) Peptide linkage (or amide bond) (2) Disulfide bridge (or disulfide bond)
11 (1) Peptide Linkage: Condensation - Condensation of amino acids mediated by nucleophilic attack of NH 2 group of one amino acid onto the carboxylic acid of the other generates the amide or peptide linkage - Such peptide bonds are the basis of the formation of polypeptide chains from individual amino acids Amide/peptide bond
12 (1) Peptide Linkage: Tetrapeptide Systematic name Alanyltyrosylaspartylglycine
13 (2) Disulfide Bridge: Condensation - Of the 20 naturally-occurring amino acids, cysteine is unique in that it harbors a thiol or sulfhydryl (-SH) group - Such thiol groups between two neighboring cysteine residues (in the context of a polypeptide chain) can undergo oxidation to form a covalent bond called the disulfide bridge not to be confused with salt bridge - The disulfide linkages play a key role in modulating protein function eg dimerization of insulin receptor (recall 1.6)
14 (2) Disulfide Bridge: GSH as a Reducing Agent - Glutatathione (GSH) is a naturallyoccurring antioxidant (or reducing agent) within plant and animal cells, wherein it plays a protective role against oxidative damage due to oxidants or reactive oxygen species (ROS) such as free radicals - GSH is a tripeptide (Glu-Cys-Gly) with a -linkage between Glu-Cys - GSH can act as a potent reducing agent to reduce oxidized proteins containing Cys-Cys disulfide bridges - In the process, GSH is itself oxidized to a dimeric form called glutathione disulfide (GSSG) - GSSG can be converted back to GSH with the reductive action of NADPH Glu Cys Gly
15 Exercise 2.1a - Draw a generic amino acid and identify the C atom and its substituents - Draw the structures of the 20 standard amino acids and provide their one- and three-letter abbreviations - Draw a Cys Gly Asn tripeptide. Identify the peptide bond and the N- and C-termini - Classify the 20 standard amino acids by polarity, structure, type of functional group, and acid base properties - Why do the pk values of ionizable groups differ between free amino acids and amino acid residues in polypeptides?
16 Section 2.1b: Stereochemistry
17 Synopsis 2.1b - Amino acids and many other biological compounds are chiral molecules recall All chiral molecules have an asymmetric C atom attached to four different substituent groups - All amino acids but glycine are chiral! - Each chiral molecule has a non-superimposable mirror image the pair of such mirror images are termed enantiomers - Enantiomers are often designated D and L depending on whether they rotate the plane of polarized light right/dextrorotatory (D) or left/levorotatory (L) - Proteins are exclusively comprised of L-amino acids even though many L-amino acids are dextrorotatory! - Biochemists employ Fischer projections to depict the D/L configuration of chiral molecules in lieu of the actual rotation of the plane of polarized light
18 Enantiomers - Molecules such as tetrahedral C atom attached to four different substituents are chiral ie their mirror images are non-superimposable in a manner akin to left and right hands - Such non-superimposable mirror images are called enantiomers - Enantiomers harbor distinct physicochemical properties ie they rotate the plane of polarized light in opposite directions by equal amounts (D/L-isomers)
19 Polarized Light: Properties End-on View of Light Polarization Non-Polarized - Light is a form of electromagnetic radiation - Light is comprised of two electromagntic wave components that are always in-phase and oscillating perpendicular to each other and to the direction of travel: electric field (E) and magnetic field (B) Vertically-Polarized - E may oscillate in all directions (non-polarized light) this includes most sources such as a light bulb or sunlight - Alternatively, E can be made to oscillate vertically (vertical polarization), horizontally (horizontal polarization), or elliptically (circular polarization) Horizontally-Polarized - It is noteworthy that the polarization of light refers to the direction of oscillation of E (B is always perpendicular to E!)
20 Polarized Light: Polarimeter The direction and angle of rotation of the plane of polarized light can be determined using an instrument called the polarimeter
21 Fischer Projection - Fischer projection is a 2D representation of a 3D molecule - In Fischer projection: - horizontal lines represent bonds coming out of the page - vertical lines represent bonds extending into the page Emil Fischer ( ) - Amino acids are assigned D/L configurations on the basis of the spatial position of the four substituents attached to the asymmetric C atom (harboring four distinct substituents) relative to those of glyceraldehyde: - if OH group is to the left L-isomer - if OH group is to the right D-isomer
22 D/L Configuration - Biochemists employ Fischer projections to depict the D/L configuration of amino acids in lieu of the actual rotation of the plane of polarized light - Thus, amino acids are assigned D/L configurations on the basis of the spatial position of the four substituents attached to the asymmetric C atom relative to those of glyceraldehyde: -H = -H -NH 2 = -OH -COOH = -CHO -R = -CH 2 OH - Proteins are exclusively comprised of L-amino acids even though many L-amino acids are dextrorotatory!
23 Chirality is a Hallmark of Life Thalidomide (sedative/anticancer) Thalidomide (teratogenic) - Most drugs are chiral molecules and only exert their action in the form of one of the two enantiomers - Only the correct enantiomer is active, while the inactive enantiomer may be inert or toxic eg while one enantiomer of thalidomide is widely used as a sedative (sleep-inducing) or anticancer drug, the other is teratogenic (causes severe birth defects) - Accordingly, the purity of drugs to a high chiral level is critical so as to ensure the administration of the correct enantiomer and avoid undesirable side effects
24 Exercise 2.1b - Explain why all amino acids but glycine are chiral - Explain how the Fischer convention describes the absolute configuration of a chiral molecule - Explain why an enzyme can catalyze a chemical reaction involving just one enantiomer of a compound
25 Section 2.1c: Derivatives
26 Synopsis 2.1c - The side chains of amino acid residues in proteins may become covalently modified in a phenomenon that has come to be known as post-translational modification (PTM) - Three most common PTMs include phosphorylation, methylation and acetylation less common are carboxylation, hydroxylation and nitration - Such PTMs serve as molecular switches in their ability to alter and modulate protein function - Like proteins, free amino acids can also be modified such derivatives function as chemical messengers
27 Common PTMs in Proteins Serine Threonine Tyrosine (Histidine) Glutamate Proline Phosphorylation Carboxylation Hydroxylation Lysine Arginine (Histidine) Lysine Methylation Acetylation (Parentheses indicate a rare event)
28 PTM Biochemistry Goes Green! Cyclization and oxidation of: Ser-Tyr-Gly- Internal chromophore of GFP Single Bond One sigma ( ) bond Double Bond One sigma ( ) / One Pi ( ) Conjugated system Alternating single/double bonds - The so-called green fluorescent protein (GFP) owes its colorful properties to cyclization and oxidation of Ser-Tyr-Gly- (-SYG-) triad of residues located within the protein core - The resulting chromophore harboring a conjugated pi-bond system absorbs visible light of all wavelengths but green ( max = 510nm)
29 Amino Acid Derivatives As Chemical Messengers - Decarboxylated form of glutamate - Regulates nervous system - Decarboxylated form of histidine - Regulates inflammatory response - Hydroxylated/decarboxylated form of tyrosine - Regulates nervous system - A tyrosine derivative - Regulates metabolism
30 Exercise 2.1c - List and describe major types of PTM of proteins - List functions of amino acid derivatives
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