1. Amino Acids, Peptides, Proteins Functions of proteins: Enzymes Transport and Storage Motion, muscle contraction Hormones Mechanical support Immune protection (Antibodies) Generate and transmit nerve impulses Control growth and differentiation Lens protein in eye Feathers Spider webs Horns Milk proteins Antibiotics Mushroom poison ….. Luciferin, luciferaseHemoglobin

2. Amino Acids General structure  carbon, side chain (R group)

3. Amino Acids

8. Nonpolar, aliphatic R group Glycine Alanine Proline Valine Leucine Isoleucine Methionine Aromatic R groups Phenylalanine Tyrosine Tryptophan Polar, uncharged R groups Serine Threonine Cysteine Asparagine Glutamine Positively charge R groups Lysine Histidine Arginine Negatively charged R groups Aspartate Glutamate Amino AcidAbbreviations GlyG AlaA Pro P ValV LeuL IleI MetM PheF TyrY TrpW SerS ThrT CysC AsnN GlnQ LysK HisH ArgR AspD GluE

9. Amino Acids

10. Additional properties of Amino Acids Numbering of R group carbons CH 2 + NH 3 CHCOO - CH 2 + NH 3      Aromatic side chains absorb UV light Disulfide bond formation with cysteine oxidation reduction Trp 280 nm Tyr 280 nm Phe 260 nm Peptide bond 210-214 nm

11. Amino Acids Nonpolar, aliphatic R group Gly, Ala, Pro, Val, Leu, Ile, Met Gly - no steric hindrance Pro - hinders backbone flexibility hydrophobic core of soluble proteins found in transbilayer part of membrane proteins Aromatic R groups Phe, Tyr, Trp hydrophobic, Stacking Tyr/Trp - H-bonding Tyr - site of phosphorylation Polar, uncharged R groups Ser, Thr, Cys, Asn, Gln Ser/Thr - H-bonding; phosphorylated, glycosylated; enzyme active sites Cys - disulfide bonds; enzyme active sites; metal ion binding Asn/Gln - very polar, H-bonding Positively charge R groups Lys, His, Arg His - pKa close to neutrality (catalysis); ligand for metal ions (Zn 2+, Fe 2+ ) Negatively charged R groups Asp, Glu General acids/bases in catalysis (lysozyme) Chelate divalent metal ions (Mg, Ca, Mn, Zn)

12. Uncommon Amino Acids collagen myosin prothrombin elastin

13. Amino Acids Optical Activity of Amino Acids For all AA except glycine the  carbon is bonded to 4 different groups: Carboxyl, amino, hydrogen, and R group (in Gly, R group is hydrogen) Chiral center =  All AA except Gly Gly

14. Amino Acids Optical Activity of Amino Acids 1 Chiral center = ___ stereoisomers Stereoisomer found in proteins =

15. Amino acids act as acids and bases “zwitterion” amphoteric Base = proton acceptor, electron pair donor Acid = proton donor, electron pair acceptor

16. Amino acid titration Curve pK 1 = a carboxyl group pK 2 = a amino group isoelectric point (pI)- pH where there is an equal amount of (+) and (-) charges (overall charge of zero) isoelectric point (pI) for glycine is at pH = 5.97 pI = (pK 1 + pK 2 )/2 2 buffer regions

17. Chemical environment influences pKa

18. Titration Curve of Histidine Histidine R group has pK a = 6.0 No other AA side chain has a pK a near neutral pH So Histidine is really the only AA that can be: an effective buffer at physiological pH (7.0)

19. Peptides and Proteins Peptide - two amino acids joined covalently by a peptide bond Polypeptide - many AA joined together by peptide bond (M.W.<10,000) Protein - macromolecule with one or more polypeptide chains condensation

20. Peptides Ionization

21. Biologically active Peptides & Polypeptides Dipeptide (Nutrasweet) Other small peptides Oxytocin (9 aa) - stimulates uterine contractions Bradykinin (9 aa) - inhibits tissue inflammation Amanitin - mushroom poison Polypeptides Insulin - pancreatic hormone, needed for sugar metabolism, 2 polypeptide chains (30 aa and 21 aa) Glucagon - pancreatic hormone, opposes action of insulin (29 aa) Corticotropin - anterior pituitary gland hormone, stimulates adrenal cortex (39 aa)

23. Proteins contain other prosthetic groups

24. Protein Structure