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Br TAs Cerzimnaa- 4— Medes. oie Liradand,(pan —Top Maj C7 Als Ale Ly Phe~ GIN Ser Aso Phe— Asn The~ Gin Ba Fics, as as Gyno ae Hep e00H ala-Cyy— Arg Gly— Phe— Val— >= ity Ls Als ue) Lysozyme 2 AChsia eT yr Gln Leu Gin— Asn Ty1 Cys Asn — COOH se BOVINE INSULIN suf B Chain Figure 326 Lysozyme and bovine insulin. Figure 327 Folded sheet structure of bonds proteins. Polypeptide strands are linked by hydrogen 4cFigure 328 Alpha helix of a protein molecule isa coiled chain of amino acid units, The backbones ‘of the units form a repeating sequence of atoms of carbon (C), oxygen (0), hydrogen (H), and nitcogen (N). The R stands for the side chain that istinguishes one amino acid from another. The configuration of the, helix is maintained by hhydzogen bonds (broken lines). The hydeopen atom that participates in each of these bonds i= not shown. (From Kendrew, 1961) 47Jattelix (peptide backbone) (Cysteine) (Cysteine) Cih—SHHS—cHiy> (Aspartiey =H, (Glutamic) S, ¢— Ci; —CH 0 Figure 329 Types of bonding forces that contribute tertiary structure to proteins. (A) Formation Of 2 disulfide bond; (B) hydrogen bonding of R groups; (C) hydrophobic bond; (D) salt linkage.A Figura 24.15 fc jiante un enlace de ‘Ordeniamiento a-helicoidal. Cada grupo carbonilo peptidico se une mediante idrgeno del gropo N--H dea sigente Inces ssl poreveran verdes eel modelo moked agus, ‘de a hélice. Las cadenas " Ro H ko 4H Ro mea fb ok a FT aly Ut. Je et ths Se if oO H sf oO H Re R Ht ° H 9 &, No Sa ES AME Nye 2h SO, I “ | | I %, | > Figura 24.16 Toutes) @ ete Be Reordenamiento de limina i, aE A oy: AN ACN CN Plegada. Cada grupo carbonilo ge { at oe head i ¥ a i ¥ CH’ eptidico esta unido mediante K o! 4 6 Hx? oO nee enlace de hidrégeno al hidrgeng 4el grupo N—H de una cadena Peptidica adyacenteoN lobular tipica wo al azaren los puntos dence ean segmentos de enrollamient Segmentos de hétice a con donde se dobia la hélice Ile Gin Nae oS ae poy once Mes Bes Tye A SR yet Oy 4 RT \peome RTS Cys“ $—S—Cys—> Pre Leu Gly+NH ‘estructura primar > Figura 24.18 ‘Comparacién esquemética de los niveles de estructuras de las proteinas. La estractura primaria es ln estructura enlazada covalentemente, incluyendo la secuencia de aminoscidos y los puecntes disulfro, La estructura secundaria incluye las dreas de helices a laminas plegadas © enrollamientos al azar. En la estructura terciara se incluye la conformacién total dela molécula, En Ia estructura cuaternaria se ineluye la " asociacin de dos o mas cadenas estructura terciaria cstmuctura euaternaria peptidicas de Ia protefna activa,xg evens def Vin ee (Quteiv) A Dihufe tor Lobe Z Reet: Lee gee é slap plies 6h fide Latiyit, ae fer ta eaueegy eahies Aa fa Stollen Wa Loge Sathae he 2 wey dyl de fi t2 A2nxoACs. 3 Bify hoa Zid EJ Leer ali _ Me —L) 1S - 4nd Gee anion tid Lin Cad x be oe AAAELESAS 1 ahaa yy PIO G* Nt ae a Pe C-NH- th o-04 73 Gali, Dr Cott Aap a ALeunfey 2g se ( flees har. Pie amr a Age 20> VA YA ‘hae ZY ase a abuvicdirn oh bith oo > Tay 1G aang, 4> te sav 2, Vo AA, We anual Hr. — en an “itt as Seen bo elev ee Pipers es fo eg eb Li 4, AMurAw 2 gpece LA Shoe ch tate Aen hoy Ate ALAM, pte Wt “50> aur be 62s ena Me> aminoa titer -