AminoAcids - A Free amino acid Common to all u—amino...

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Unformatted text preview: A Free amino acid Common to all u—amino acids oi proteins ' Side chain cut-Carbon is is distinctive between the for each amino carhoiryi and the acid. _ amino groups. B Amino acids combined in peptide linkages —NH-t|3H-CO-NH-il:H-CO— Side chains determine properties of proteins. NUNPDLAFI SIDE CHAINS H | +H3N - c * coon-I 1H} mg: 9.5 pK1= 2.3 Glycine H +I-I3Nu-r'; -cnoI-I tin-:2 .CH ch CH; H | man we "coon | f. .. F. C I1 .I H *H3N—fi: moon CH3 H ‘HHN — C —CDOH H -- c CH3 {:H2 CH3 Phenylaianina UNCHAHGED POLAR SIDE CHAINS H | man-1? —CODl-I H—C—DH Aaparaglna H i *I'IEM—(f—CDGH H — C —flH | CH: Thrauninl H I. *I'IEN “I? — GOG" CH2 I «31-:2 4“: “N D +113” .1 H 'I —C —CDDH ,I X | WIN (3 — coal-I T pK3=1ELB f vzm2 I| SH-II— pK2=3.3 Carmina ACIDIC SIDE CHAINS pm = H H | | pug: 9.8—-*H3N "LI? —cooI-I pK5i a BJ—I-JI'IaN—i? moon CH: C. if} I u ‘an—pKE= 3.9 04/ ‘OH ...— pK2= 4.3 Amt-II: anld Glutamlc acid BASIC SIDE CHAINS pK2= I92 mam—H 0 cant! I i CH2 CH2 GHQ {LI-H2 '7‘": cu2 H — H MIH3*--— pK3= 1:15 (I:_H|-|2+-I—- pKGI 12.5 | NH: Lysine Arglnine 5 Polar aminu acid: "annular amlnu (l}duIHrun alumna} {Hunter flu Iuflm an “1! Eur!“ a! Wandary amlnu Primary amino grnup grant: {EH {h +H2H — (:1— CUDH iH:H_.E: _ 30m I “finch-EH2 6H3 mm; Alanine Cchflfllll FDFIHI 1 Funk! ll {m min. 'HA‘} Equlflllflltl DH- iddld H H H +H3N c coon High] c {300' H2” 0 000' 6H5 CH3 "\ CH3 may: I m FflFIH u m Fun“ In pic, = 2.3 mg.- 9.1 Alaalha In acld solutlan Manlnc In nautral aclutlcn Alcnlna in baclc cclutlcn [pH Iaaa than 2} {pH approximately E} {pH annular than 10] Net charge a +1 Nat charge: a Hat charge: *1 {lsoalactric farm] [email protected]" - *HEN—é-CDD' 3 once ABSORPTION I At the pH ct tha atcmach {1.5}. a drug iikc aaplrln [wank aclrj1 pK = 3.5] will be largely prctcnatad .- BEAHBMTE A5 h BUFFER {COOH} and, thus, uncharged. . Unchargacl drugs generally crcaa [HUD -] nLcrpgbggnaa'mt'lc rapidly than I H: K+In ——IL ._ ca moccucs. P P a [HEEL-,3] ‘I I An incraaaa In HEB; 1; cauaaa tha pH tc rlaa. I F'ufn1r.:lnnaryr chatructlcn cauaaa an Incraaaa in carbcn dicxldc and cauaca thc pH tc fall. rcaulting :_ in rcapiratcnr acldcaia. '- r . :.|.'l' lit-b; CD: + H20: HEIEEI; 4:" H“ + HEW Amino acids (fullyr prolonated) a-carboxyl group [-GOOI-I) deprotonated (000‘) at physiologic pH Nonpolar side chains i in the interior oi proteins that function In an aqueous environment and on the surface of proteins (such as membrane proteins) that interact with lipids in proteins. most a-COO' and o-l‘ng+ of amino acids are combined in peptide bonds. Therefore, these groups are not available for chemical reaction. ' Alanine Asparagine | Glycine Cysteine Isoleuoine Glutamine Leucine ! Senna | Methionine Threonlne Phenylalanine "Tyrosine Prollne ———' — Tryptophan Valine band Side chains of 20 different types Acidic Basic side chains side chains Aspartic acid ' - Arginine Glutamic acid Histidine ' Lysine . . __ _ . T __._. characisnzad by characterized by Side chain dissociates to -COO‘ at physiologic pH found i in a protein, particularty . . . Thus. the chemical nature of the side chain determines the role that the amino acid plays Side chain is pro- tonated and generally has a positive charge at physiologic pH found i on the outside of proteins that function in an aqueous environment and In the Interior of membrane-associated proteins Henderson-Hasselbalch equation: pH = pit, + log EJ- [HA] predate P" = PK. when [HA1 = [4"] Structure" _ ' 2— of Proteins — — — ell . . . how the ‘ -'-_ protein folds __ __ _ ' into Its native -,- conformation. _ ...
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