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FEI AO A AE CE OAK A PRE RRA (RA ASF «LS A WA AR HA FEA. FE IM ROK HEB EA AEE EE 9 M,C AT Met 9 R BLA AA S 1 FF Cys BAK SE pKa 29h 8. 4,870, Cys EAM pH FE BLEND Cys FZ PAT AD AH AE BE A FE A FN A ALK HEE AR i TERRE i Cys a te TE Ae — i481. Met RE SRF (ARH Oh ABA SE he BB AAR HE AY CATA SE IAG Met 1 2 TAR HER IEMR, Met MEARE TP ARREST A HO AR He Oy a PR ES IFC FP G) FERRER APH Tyr Phe 1 Trp, COM REARS AER ARE BRK. ‘ED ALE AE CAT AY a ae RA. Phe MARE EAE RL SE ERR Tyr AIR EAARE MES SAMO MR HCH RARER Trp Oe EO Be IER EY NO FHS 5 BARONE PRL E ANH AE Ht Phe Bh. A) SRO ERIM FILA Asp.Glu,Lys. Arg A His, 0 AAA Ae RG SH WEB. Asp #1 Glu ARH MERRIE R AAT AAT AG eA DH FR TA HB AY s Lys, Arg il His A wRtE REM. CMH RRMA AM NRF EAM pH RE pH FRR EMER, Hist RBA &N BOKRER Lys @ ARMY eR Are SMILE, BE ROR R AIF OY Ee ARE Sa ‘SA AE Ci A A MR RAL A AA Fb A I SN HERSRMH RERKSSE RMB. 2. 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PTH AR aE SE (Edman BEM) POEM FUE ES wae Ps a RES SOR * OER a EA RMR RP MIR He tRNA, BMR-IRNA SR, BBE-tRNA. BG BE ATP & ARE & Rem REPREMNSSHRT Foe ROO SGM INTE HE ANE At Pro 3 a 64 RE Ak SAMA A A ROE s0000 1. Trp.Phe #1 Tyr #38 9b 6 200007 71\ Trp.Phe Ml Tyr R= HAIMA MERE G47 10000|—} FEAR BAER EAT AEE IRIN(230~300 nme eA =, 500 at ASCARI, tO 1-13 FAR Phe A Tye Home 2000 4 r\ MAL 280 um, FA REEMA 1 "4 RADAR MAE 260 om), AM LRH MATA EO EMME RA. roo 2, MAEM R MS 5 OBOE so Pe \ S14 RA TO ET A 20 ROO LI ME ML PAE IH AA AB wet td Se LA a EA EE vam (D SABA Ser Thr M Tyr SHR PHIW13. Tep.Phe #0 Tyr MAR SHIREee gua + 1+ Ri-s MERMBRAOR TER wx BRA Pt ie rercty oR MAHAL “aes Are Met t-S—CH, 1,0; ates seem EE Cys SH CZ a Ze Bet His aKa RMA —Pouly HAL eaet Be His Tye 89808 RAAB — Pauly BEAL whee BE Tye Tyr 9 Ie RM —Folin RAL meme REMAN Tye Trp ORR IE HIRT Remm BET SercThe Ht Tyr MFI RATE armies ma weet ROOM, RAAT FTE RAMS SS RRL. Fh AP AO 19 A 5 AT S E (2) ATRL —SH A MME Cys HAA RAE, HAL TT BLE Wy AE SS Se A A A 4 Cys SAT RE ER. SOE TS RN SA Ry SS mineat), 3 ra i 1 as Nite E —~fxi—cH—c 1 cH, cH, I I st mh $ | +H1,0 a ER § 1 | cH, cH, i NH—cH—c. | fv cx—ef ae j 1 ° l Ql TERRA RRR (3) AAT OR PIE RIE His MYR AAT AAT A A AR AF Cp 7) BEET DA Ya F932 A TH 08 BE EE HE eA His coo® coo® e 9 @ WN C—H HN C—H 1 | cH, cu, - Os at (A) Lys ff e—RE Lys 8 eR th AF DL Ft eo a RA BS Se A I SY EE LAE. Ea A AC Dy RAE AR A So — A SR TTS BLS es SE HR.112+ S-m@ ZORNBAS DE =. RRMA RE RAMEN. D HMA SE OA ELL. De HA A ‘NB | NO BO HER Are, $A PRES I AEH Trp. PE PRE a. Oe RE RT HE — A aE A RR AIR OA HES TR ——GABA, © SUL SE APE ATP. © fe eESEE HOTT. EE ssensmsecee BRAT Ke FEN YE A RE EA A MH EC 8 A C0 EB ER Ze —. Rik AL Bk Celectrophoresis) #8 AO BURL ab 4: SbF AE SME FFB TF «(AP AL a EH OBER. GIR AERA F aS FA Acs TEAR A BHSDERAG ME TO IMR. RP SAS PAE PE MI BD FAC Ky TEAR AP FEE SE BEAR AA 9" 9K "I AS TL TT 2 A LAR EID TET ATS ER BA STN AR — BALA EH IT Alas Lys. Asp SPM FERPA Ft UK Cfree electrophoresis) AA XE 4540 9 KX HF th dk (zone electrophoresis) MAK. He C04 Mk AEM Tk KP AB 45 A a 3 i A Dk LE A BRE RB Hy HF RD «LB LR CO ARS LR ER) 3 1 OE Lys AAS aut Asp mts =D REP NS F IER MR A FM DRE ETT BASH. ULPH 1~14 95 fl AURA Ala.Lys # Asp Ai EH 3k FURIE TE DH 6 AAR MERE MP LIK ABZ Lys 1 Asp BAe pH 6 28 ob E MEY 4A A AA DB FUERA TT Ala ESP ADF pH AEFI pl AVR MATE HHH PHL A IE, ELAR MAE Dk wh. =. Rit JB 8k (chromatography) EE 1903 5F 9 CAA IR A 4 A Mikhail Tswert AUK AA HU CK HL CB AR CHM. BRA HY RR OF eA oh BU AAA Me. — PAB A&E A stationary phase), 81 DLE (AMA BE th BT ELE (Bi Be BB — hh MA EB HC mobile phase , MAK AA ANE AL. ‘ARE PE a OCR RN «SD A CH, EAA GG AF 8 Aa AT EE Be ALE A A PE DUAR PEAT PED, 5 Dae ADH 7 RS A Ey BERR s LZ 5 5 DE HATH FARR AA, LT 945 AA — AB Sh AA TGA 9} BS A AH SY BL CHE 1-5), FBTR ARIS ME LAE A A A HE TTT Sh MT A HE A — VAs AR A OST EAT Sh A STC ERE BEI-14 Ala.Lys 1 Asp ADMLaR AERRi-s SEORHARAMED Re Bam + 13+ i EM _ co LS Ae 1 PA I a FRR ‘e150 AOM A AR CLE 099 RE LO WERE EMME SIR ALITA AR A GF SIR RI REE AEH AL BEWR, HeMLIN ODF AA A LOL KEM EAA A AT I A AE HY ann SE HE es — FS Shes A IH EL A RRL BRE AL A IRD PEA Sp A AA HE RED EAT TT LAS) Ra RR I EB ‘RUPE ACHCHUB HF (high-performance liquid chromatography, HPLC) . LFF SA 8 Fe EE A «SF 2 HZ HF Cion exchange chromatography) A247 (gas chromatography, GC) #1 HPLC. it Ht EWM FAR 1-15). OF RT ALLA Bee BE AS a SRP ALB oO SF 24s Se HE ATT TT. MEAT AY Se PF FT ZR AE CG. PERT FRR AINE BEALL ‘EEPROM AE TF PR a eh ESA AAT oe Me a A eS Be A Ao 9 A AT SH RS 5 (EB FL SB SH HR. FAFELA Asp.Lys 1 Ala = S136 OR 5 ON. MN Ra FHF 3 HR FTE DH 6 fA ah MPEP BE BB 2 OE WAY Lys HG BR AE Ait» AF HA A TY Asp FURR HB AG IE AY Ala Hp BLAM HH BE TE OE HH Lys Se AL A a BP AB EMIT Lys 5 Asp il Ala WLIW 15 FRE Sr eee OS RS. ORE BENG Asp A Ale SPIE «AU LAE 3 9 FSR PEE 47 BSP BT. nhiintti the —— B= tM QS ymuce. edu/ ~ plarkin/4301folder/ HTMLCH5 %20/ //web. indstate. edu/theme/ mwking/amino-acids. html 3. http: //pubs. acs. org/cen/topstory/8021/print/8021now1, html114+ 2-m@ ZBmNeAS WE 1. Barrett G C. ed. , Chemistry and Biochemistry of the Amino Acids. New York: Chap- man and Hall, 1985. 2. Heiser T. Amino acid chromatography: The “best” technique for student labs. Jour- nal of Chemical Education. 1990, 67: 964~966, 3. Hao B. er al, A new UAG-encoded residue in the structure of a methanogen methyl transferase, Science. 2002, 296, 1462-1466,$s ZARB KOREHSTRERA MRE RT ROS RY. AMEN. — Re ot SEA SSB HS AD oy, eH RR He EH ACTS RACRD RRS «AF A 2 eR RB EH OT Ak (peptide) iE BEM 2 (Bi St a~ SAE i ~ eH HZ LL MMe HE Camido bond Bf amido linkage) AKER (peptide bond) 48 i A 4%. (LH BAK (oligopeptide) ,# kK (polypeptide) MH AM. MRRP BRAL(ILUEAR A ACMI (residue) . 28 A RRIRAELL BRAT LIN BE AREA HRB WN BLE peptide chain) , —. RHP RABE AR A 9 3 A A A (—) Beha BRO 5 SS PT A SI I 9 GS JLB. BS 2 Tk Ps — i 3 AH BURR PRA = BR LBS HE CE 2-1). — RHE 2~ 10 4h AE AR HE A AL PRN IR ohh 12~ 50 PEAR AGL LK AS 90 eB 50. A (Wak wie I IL aioe mete i i | t i ov) x en—e-byn—en—Lan—cn—L—on (cH @em éxon — dusn dens, sex—Cys—Aso 5 Sam enERR em Bo mMIKHEAHY BT DSB SRAR AK BE LE JU AB AR EAB BAT AB AY SEP AE A — AE A) — Ey Camino terminal) a& N Jit» 27 Fi tt a— IRR 8 — S85 Wy EAE AH (carboxyl terminal) Be CM. (A — HEA BE (NE AZ. LT a A] — SR EY CS BU116+ 2-m RORNGMS De (=) RMS ‘REAR AR BSS — A AC J DAN 8) C5 BDA INH AG CAL TR NSAI C OPS H AT OH, 4 RAR Se aM aS tem. A 2-1 PAY = ARTS Hy Ser— Cys—Asn a H—Ser—Cys—Asn—OH ah SCN. (2) Kee IE 6 A A BG 1D HAE HMO 5 SAN 8) CR REO SE SE oe A. SELIM BE 2-1 8) RAMS KL Sp Be & HP SIE eR 2 HE SE BAN HY eZ — A A A aR / EE «I I EF A FR A 3 RRO AMS ER Fei A MK Be TB 0 A AA A 5 a 2 A HE RAR TR. ‘HB Sk I BB R.A TRANG CU N 9 Re — A HE (peptide group) KAKA (peptide unit), BEEZ ABI LL F HED: 1. SOARED ALONE DE 40%) SEARCY 0. 133 nm, $F — 7 AIL HE A IB (ET AA AY MLR HE BR RIN Ths 5 A SBE BE SF AY CRI 2-2). 2. By BE Cerans) LAO Cois) «He aK YI 5 Bf A 8 i Ly TT BORE. AR TIT, WIR AR AE ohh — FE BR AY BRAG Pro) WE SAE TE ALE) CX— Pro) , HB A 3 1 BE AT BE AE 2-2 ake meet 2-3 X—Pro 2 mA LK MUM SK AK 2 + HB ik BL Po MK 9 Em i A) LH OY a B EMC 2-3). Pee Be eC 8. RRB 6 ANUP Sek Fh TF me raat NC” eR REF TH Camide plane) at Bt Hi (peptide plane) (I 2-4). WR Be FT SA 1 OF A ES TE BE FE A A 9 FE fT — 4 ER AEA 2 4h BET HE 18 CoN REE 9 J BEEF BC phd .Co—C SALE HY fr IE ME psi), 4 AMAL ARRM REM § My MEL JG ARE ER OU AE tT ESP BR #7 y BS MG SEAN Sah C3 BB DAB BB ARUCAE # Ny» ETA Cox i His FF CA AF OD «TE REE HRSA FAA oy HOTE RE TRA FM AE LF $y SRM ae TAA A mL A 2-4 REE a BH If. A Ay "0, “ ®Roe ROHS + 17 + AB BAHAY BT LEA 8 BA 0 A A Ee eS 3 PRD Hs HRA 9) Ramachandran FEMME. Ze Ramachandran PAL} RAMAN Fg) RAP Ths, AGL 6 Hy ATVB O° ~ 180° 9 EE fo EL os FARE AEA LA 6 A EL I AS. HE 22 A BE Gly (9 OYE REAR Is BLE PE OY BIBL i Pros 9 5 38 hy 4. NAP RB SP TE af «OAPs A ik tA He NV Ef ts 5 AA RP He Sa =. SROHBCER 1. HE Die TAF Te A TL 4 eo 1) NT SA a a A FREI ie HE a HE. AP A we wm He 5h AGE a Ea AA. LL PS «oe a a eS AG GS SiH pl RA eS RO es BE A AG 5 CA A — A CCF FAB FB 2. a OR HE RE 5 Te A) HEL 1 Mp Oy BR AZ Miz (biruet reaction). MAF I AE 5 EB AL CE ATP FLAS MARAT) A fe 8 CPR 2-5). SUPRR OR EE HT ER aero FRE LE IE SAT NR ER HE EA SOR RAMTEC 2-1), EEK ALPES 2-5 MANDI $y FREER A FAL hh DNA 109 BITE DNA SF RA aA. (EERE SRR A SATIRE LA es DT Aa 1 BO OT OS FFE BAM LIN Te oN OI HT BE HK Cglutathione) AIMS FEMUR S t/a Fake. R21 DERMIS Eur 5 a hie tk ROT E AR emit te =k BORE A Bm sam S: a FRR Bk ot oH D- Rem 4 IU RNA 4 BIL Pc SIRO RAM aaue Auk mh sa =ak a) aH im wel th ek AERIAL FL ik PRR mF ee ER PR RUE IKEA Aik aaae Ee maar Pe Fra ARAB ete mi ak avs mk a118+ 8-m BOmMBMS IH Ea bey BARNA BEER 26H — RSA AT Oa «BH A A CL A (A SAD RAE DD «2 Fa A a AA RH C26) e0-Gly-Ala~ ® Seen (uc 6 6p HE) sae (ail ie) 25 Bes Bee A He —. BARM—-RaH EE IR) — 2824 #8 (primary structure) tem He HE AY SE Ot SH» HE SA A AOR — 7) BB — AO — LO A. 1954 4 Sanger 151690 5 HBR 8 ME Cinsulin) 9 —2R SAY CFR 2~7) Ay Ht 9S — fe 2-7 ah Ree — RE Hywoe Bammem + 19 + th SAH VTE. Sanger BUSA AR 1958 SET A AE 1965 AF 5 RRA} Ae HA BE ERA A TSA A AAT Ar RE BARR LE: A ER UE ee AR LTA ACRE BE T Sanger UE tH A BS K-S4H REM. se Es A Hs I @ Aadike aaa ee (mh 2-8 a BRET AU BRIBE EO = ARAN HCD A SLM #0 = AAC) Ba a EY — 1 BSH A A A» Hy A BU WL BT Be se DEM SR A I, 5 RG OR 3 Ee A I, RT A A (DB 1 Fa A 0 6 A HS) TT AA AL 71 A A Hy «LA HY EE BA 9 BEAT 46 16 A TR RAE AAA PLAYY PEDO, A FLAP CLactalbuumin) A199 BEAL 9.916 5 FT» AL A RE EE SP ALLER 2— 8) 5 EL 5 2 > I eH Vee am He ea TU A TO — RSA RET GL AR PF HH” Cmolecular disease) . Mui 20K AEH SeESPACHE p MEAL 6 {0 Glu Be Val FA, BAIR A EAR A A PE 5 — WF a FE AS A) Ba A aE A LE A He TB TR (8) — A HT DT A A A A «I — AA =, RARHI RAM BEET MLO — BAH (secondary structure) fii S Ake HEIR AS A ALA R AHL TE ML EA 1 A Ea SA RN A AZ 1 5909 — A HAL MEE (alpha-helix) . = REAR ME (triple helix) ,p HFA (beta-sheet) 8 HFM Cbeta-+ 20+ 8-m ZORHSMSIE turn) 8 Eig (beta-bulge) #1 EAL # ili random coil). (=) RES 3,5 MR a OR FB — AR HE SL — 9 HY HY Linus Pauling #1 Robert Corey F 1951 448 4) ICES Je: D BRGE APSR BYE — 1 HHL HE Ya CC 29) 5 DSIRE RL 1 EY ICE PPAR on CR AE 2-9 a MUNEEA NI JL Ae a: MELA —C—O 5 m4 fRRIE EAN 2 (OLE SLY AS A PE I. A AA AT 3 Fl o MRE HL ARI 3. 6, MRE CEN 2-11) :@) AF 3. 6 PARI RE LTE I, 7 RETR AL EEN 100° ARI HY 0. 54 nm, BP AEA RAYE FE 0.15 nm, MBE ATE Hy 0. 23 nm, @ fh AY fh SPB R417 D co MRALFAHF ZH RAPHY o Mie ERE ER We (FH 2-10) 5G AMR AE AY R AEA LE FMR BEY I | IE AS SMR He ATE HBL. AELSEK AAs FEAR A AE ALAR AS 2 TE A Ble A By SARE SL PF FM a SA HG RE — Hh” BC A HE 8. XE dipole moment) At 39 — 7 HPL BIE. UTE BE IN Si HABE AE C MCB 2— 12), ATR HE ZF A A PAB ETE RE A — PA AY. RTT RE AT A A 4 a A 5 AS Te SB le SAR 5 ak A a RE GE 4 (EIB Fa 09 J ft A AF a 4 A a i eee bree NS BAY RHE SER COR FH Fa) LC OR AP TE 2-0 gem rE AD RABETE. SOLS RE OH «BE A eB OY SY ER SEL RSS AR FR LF Ze «Ry ARE A A: 9 SR eit Z MRE A SRN EE ET LA MR WEE (helical wheel) (FH RRA. AP J Ie HES eH BY — A ETBoB RERHSH + 21+ 2-11 He a tees a FB SURE BR PC — Ae A DR CO"). RAR A Re Me A Le — HE FB 8 ef A He I $9 100 — AB HS — 8-H 2 RB AMR AAS HARE SBE 100° SRL LH ECS Reb 00 i REAR RAC RR FO AE A, RK NE “1 MMOL AOAC mL. WM 10 Geom IEM Hn LY ARAL VRIES LI, t {vee MEE ERE Ts RRM Tey | fT LA AA ATA ME BH 8 BK a 10 SB AA AR He ME We Le BR HEA AOL k AA RR A eK BY BK ce RIBERA UP Hw HH He UM WK AA MEAG BEL A RR AES EA RE 7A AR MA A 1 — Bi: Sen ene DHL 2-15 a EE I OL ok Oi A 8 A A ER A 1 KF — TS EE 9 ARE Comphipathic helix) . REAR NEO BE TE SBA 5 EB KTS ACH PD RA 9 REE SE A A 5 BR A RK A A EE (G0 sl a HE CAA Cpolyamnino acids) FTV BEES A AGM Eo EH EL ‘et 3 RE RRA SES SAA AE BY RE AHR A LR A AE MUIR HE HH 7.0 BE STE RASLABHH Ae pH 1. 5~2. 5 OJ SEMI wo ARNE, ALDH pH 7.0 Rf Asp FH Glu fi) RAE AIAP HUH i AOR OIE FR PE ETE REMY 0 MRE (ELLE pH 1.5~2. 5 YR RCL A A sit a MRE. LPR RCI AE DHL AGF 11 A SUE AL A ACA yA ALA ELA Wen pH 12,36 R AREAS PEA A BLL LTE Ro MRE. 20 AA A PERL 8 AZo MRE HA BAY RCA AE AF « Ala Cys, Leu. Met Glu, Gla His i Lyss BOF o MIE RAMEE Gly A Pro SUSAR MAA ALF o MET AY AERA Tle.Phe Mi Trp: BK AP 8 SARA JM Glu Asp Lys Al Arg AMIE SRA te ART: « MRI LTE ORT a MRMELAI Pauling HEMT 30MM 2. 2, ORME x UREA HY Me Sh Le RR RS Sh FH I OY = ARR ES LRT EY). ICS yo ARN o EMME UE EES ME SRA 1 REALM LAY —C—O 45 n+3 (LARA EM) —NH—2 Le BRA AE BE 8 IE 3.6 (VRC RERGIR AK WC PAYER Ar AP 10 IF 2.2, ARNE HC ERAS 2. 2 NA A En AURA AREA ECO 55 +2 {URBAN 2 A SE IS 7 a ME QS 4 ae AME, EAT 4.4 PRA ACE AA A EMR AEE C—O 5 tS HRA EA NH 2 (A UL BURRILL 16 IE. PRE JURA BT LAE 1 SLE AY AB) ELLE AP AR Eo RE. A A Ni cme122: Sm ZOMNSM SDR Aspis3 BB 2-14 pane RE 5 BREE AB At 30 000 eH AAR ME H BREESE RIUP ABET a ME, FLT Bo MME — BIE SEAL DET HY 3.0 ARNE MELE — AE AY ARTI EE 9, ARE AF LE EULA BRI 2.2, RAECERL 214), (=) pire 8 HAR (P-sheet) LAW 8 HAH HE (B plated sheet) iE Pauling Fl Corey MER a Mie Hy a te PAE BLO SA — BE A = RH, A A — A «eT IE. AR 2-15 a IEE EAP AI «Dk BILE FAA FZ FRA ATAR , © AKER SRR AT HE ALK ER] OK IE oR IERoe BommeH + 23° Bi 2-15 pame ARAMA ZAI IBRAKERRL AW BARB strand). AMEE TAS AF LSB BEF SE HERE ATA HO D BRB FF 9 a 4 PAT AI PR YN — BT Hy ATES FRE RATE RY Lit N—H—O STF LP FA EA OT RE. ORF 45 B PAROS AEN FT 0. 347 nm IEF FEM SARA. FE 0. 325 nm. B FH OY — TH A Gp) FF(— 119", +113") 2-16), ERR QRH sea 2-16 FT PMR RT pm MEAT IL AS AA a Hk — A> BRE: A» ATG So AC Ral Rap). AUREL EA B ARTI LIRR A — ie RE ts FAH #8 HH extended right-handed twists). 38 #F124+ 8m ROMMBMS DA SEPT BR LE — A — SL) AE HE FS BH 2-17), ROR 8 ARSC BF Ab BA HE eM SE ER AE BB LA] LUE RAY BOT. AR AA HR RR HE FL EA(porin) k. LEAR AREA, Ih wt B DARA AREY B HLA HY Co barrel) fy MUTE St it Hh OY FURR. EB ARGS HP «AE HR A OB BOR BIR A HE REE BURL FPP BR HE FRC 2-18). DEFERRAL 5 HE BT Rh tt BO RE a AY WR A Val le,Phe, Tyr, Trp # Thr. pam AT HEA LEM 8 RR — aS KE E88 o MRE Ae) BARA SE BERS Malar a eM AHAT ALM LOY. BG FE = i ke ye RAR 9 «A RM EB LAE OR 9 A Re AE A A I RE 7 Raf READ Rap ACAI BATE wet 2-18 7A me a me A MRO mA Hy 898M 1B AR B A oh Cbeta-bend) .8 FHF Cbeta-reverse turn) . KH MH tight turn) ae I 4 #8 Chairpin structure) . i Ahi HY ARTE (A FEA BKHETE nt 180°) U FELT. BHM FLAT IN FARMED AREER LL 180° Sr RU BCT ARE AIT Dh RAE Le Ut S AEA IE eC A ERR AA —C —O 5 nt 3 {AE WRI AE 8 — NH — FE URL sD Gly #8 Pro 2 BEE Ak AP HY Zo GR AR AD Gly #4) RAB AEE NESE 8 AP OY CBE ES HE AA CRE I RAE) FA) TE RY TT Pro AE HORT AN EE AO FRR HY AE OY 9, TES ARI AG OEE MATE AD ALE EG BAAR OTE RE Wh BGM OLE T mA AE PEE A AO RR A PE BRR TEAR BE. ASAE 2 FE HAS CT DAT TT DFE HLL EP RE RE A BO HE 9H 1 CHASE 180° 2-19), 96 = APE ADC DAG HE — AB PAP — 607M — 30°, 5 8, HEAR. 1 US A HL Eee vB +3 ARE TL AE NRA An +2 RAE RE Pro, EHC 1 SGA Mont] B Pro Al n+3 Gly HAA, iM n (MB Asn, Asp.Ser fl Cys. EA ACD MY AS YL 2 HD ATA Fe A I PH BT BL SHS tke HAH 2-20),wamnem + 25 + WH 2-19 Wis pe Mm AEE Ba 2-20 pm aC i ef UE LT (8) pa SO 2—21 Bir +B ae AR a Fh ST RR IB PB A — 4 A OR HT BE TRE EO — A RY. BEM MER PT BS 8S S60 BR EE AT WY BITRAI ZS P. PME S IRENE A BA126+ 8-m@ ZORNEW SDE Aa RTD HR 6 Fam Wea pee 2-22 SIE HI EE Ramachendran PO 55 (#) a0 ‘eB Bh ie TE As 9k 9 A — me a AS — a HB a Fe HARARE» AA i LE EA IR RE A Sib) tA PE ACRE BR 2-2), ULE 2 FOREARM Se BES HH HR CE Ramachandran fA POS — Oh, MN. TARR SPEDE EAA a MRE HE eh + ORE — ROR AEE). 2-22 aR AN RS Re A Wet) SR A. DAMMREE LHF o Mi >PHR>U MAH EMG KEL RE SS FROST He Pi Wo FEMA a FE 1 EE A 8 AS AE. R22 ABI EMH HM ai ° * iat ’ RE = 180" +18 EF Mie =o BORAT 8 oie 139° +135" Site 26" 5 8 oe ne +us Mie 40" AF o Mie =r =a"mom womeem + 27 + =. HARM ERA Te We IE AY eR A EO RAL BNE SER SAI. = MER HA HY BLU motif) FEA YR (domain) A, BES SERRA JUDIE A KF TE J PE CR 2-23). A SR = SRA TE RED BEE ° I —c,—cit, — cl, — cH, RBIBO-C—cH, wre 2-23 PRS ON I (—) BEERAAHKRS 1. Se REE TES — 7 SE TRO ORF CO ah ND Se OY ARH SLUR AASB ATS — PAG DO FH HR ERY RF Chon OWN we FF AS I A GS RRR TE ‘Hy EFA AD AM PM RR NY AEA 12~30 kJ/mol He HBr HE HH AG SHEL oy FSD hh HH 5 A IE ARRAN MRED A RATM. 2. PE Fae EAP AL Re OY BE AL] PH 3 J (electrostatic interactions) JURE IH 20 kJ/mol , 7H A HK Sp WERK ARR (salt bonds) Bea HECsalt bridge) . ZEAE HE pH “F , Hi Akt 9H HE Me RR A BE AP TE RE AR AR AE UM AE. SR SRE TRGAY NO AE WG A AC A AP Eo AA MN Ts 3. BK ‘aR HE A A A: ee RM RF ACA TI A — i 29 hifi 7k 8 Chydrophobie bond) WAR BLAC AEFI) FC E-<40 Ke] /mol. CE 7k HR E11 eR BABE SALT 4 BE SLI MR ei WATTLE Sb A 5 A ATT = Ho REBT ih BE AN HEAL. AURA Se A TA ER EAB A A AK AY «BF oh RE HT HE128+ Sm ROMMGMS We SPA. SOR — Pe RR A AS a OH WB 4. fame FEMME A CVander Waals forces) EB > 48 6 97 AF fi 8 4 HEE non-bonded atoms) 2] HE Ay AE FAT fe A Jy eT A. RSL A 9 A Jo OA A Ay a 31 2. HAE induced dipoles) Z fl 9 LMR 3s HR HER M6 Hy BE AaB 7 Ao ‘Ae A FAR A I A A FZ MA S| AEF — EZ AHIR. PAE AE AE RAE AE 0. 4 ~ 4K / mol ELE CS RH AEE 5H 00 8 PL A 5. FAR 4 KR FE ft Cmetal ion coordination) fe SUFEZE F @ BE EI (metalloproteins). VURAKAE A Ccar- boxypeptidase A) fil iil 307 (> AEM A A Ht 9 A I Re LRT «SS REA Zn ANI His 69,Glu 72,His 196 (8 OWE LA Be 1 4h 7k SbF We 2 I ER AT — RE IER, (=) RE RMR ASE BE BES RA A 0 EA AX YR ART BY REAR (Nuclear Magnet- ie Resonance, NMR) (8. PURPA 2-275 A108. Abr Ae Be A LB — AE BO AROSE BE AL AR A A RO A Ae AR), UA BLO AT 45 X YR RE AL B09 IF A FF, A GE HR Cinverse Fou rier transform) 3: 44st FE BE FEB Dit = 4 9 COM 2-24) . Bey AR A 3 FE BE RAS FS AREA HE Do MH A A ah FA AT Me — HE ME A EARS Rk Sh FASE ec FG A LA A A AR. 7A SU HE AF a A CEH; Kurt’ Woothrich #80. ET UIE RY “ESE eM A HR BEE 28 a eB A LB AGA BEE SE FH RO EO. Ar HL EE < 120 CR SE AH TE AIC, i] X AR AAP A a La PP KAO FAK 1985 A 9 — 4} a a Hy tM ELA «8 48 JL A 9 6 Da BA BLE EH BC 20.6. CoP AE NMRX RAB BRA ML C1 RE HA AR Lt — A 9 (20 a “EAL BG EAS — FT 9 A AR AS DS Ra 220 X Ap AAT =RIB BomMGH + 29° (=) See ®: AeA BE a MH «A II HT SA LFS 8 BEARDS RAR. ILIA LY BUIRIAS AR HE (wire-frame) BEAD ERA (ball and stick) BU HES (stick) ‘BUS IR FE (space-filling) BEM AE (backbone) 6 #12 Hf (ribbon) BEE CFE 2-25) « mM a ear W225 ARTA = MES OL (a) 1. BU ‘BEAK tL RIE IF te Hy 9% (structural biology) LEAR BLA PAAR LA ADIE. 38 APE RSE A LAE (Ee 9 FEE, Es IF HEE sequence motifs) KL 2-26, Bi Mi, 18 & DNA 4% 4 HE (DNA binding proteins) tt) — @ #8 #) & A — BE CXX (XX) CXXXXXNXXXXXXHXAXXH FFI CK {Cf fel — A A) «SS oh 2 1 PE FC D+ Rey ME eS HA BS A Hoe eH = FE HK H1is57—Asp102—Ser 195 FFF] AL EE FAB (2 9 A AR 9B De SA a a yA Hh — BS 1 AT BY — I HE — A ES EBL functional motif) ak £4 HUB (structural motif) A824 FB = 8 8 A HB 444) (super-secondary structure) . oC R226 RE ARCH BLA CA)+ 30+ 8-m@ ReRMSW SDE ASABE Pa Bk HAL SP — eH SH He A FA A Erte — i HE UL) Zs SR PT Re HE OH a FBSA aa.foB WI RR SE. SCHL TF AAR BHR OM i 55 A A AL PP TR AK WU ee PF I Ti. ALAR IED AF BME —3 HF a MELT BI — ARIE Re FAB OR A 8 © BF MRR—3 RAF o MRT BRET FONE, WE TEs © AEH MBE coiled coil) Hi BAY 2 RAT o MNES BI — ARIE Ah A FAM ARNE sD MIE (helix bundle)— 44 o MAEM RAED @ FAR —o MNES AE BD BoBs © B AIEFK hairpin loop)— PH KYAT p Meh —THHLE sD a MMB FE ae ARBE BD ofa: ® a SBE -F—a ME s® Rossman Bel (Rossmann fold) ;@ FRI BUA (the Greek key motif) 2-27), Ae AR A — FT ARE A TS A T.-K A (BARRE Lew) 5 7 > RA tt BL — Oe A RI ok A — a. SOAR PA 2 BRE AL OCI Cheptad repeat) fA) FF ZC AE PF-AT i AE MR ME (8. HBL PFD: wt — 1 0 8 CHE 228), A i MRE Py = a BT 5 Ee SS SI EA BARAK MTB Ee AR, oe MBE — Fo SRE Let EI EF 44 CEF-hand) ih E RHE FRNA EZ — RR ER SREB AS Ca SB 2A) Colt RRR EY LB AEN ER Be ICR GR SP SY fT RAE SED Cal ER ES BARBS 2-29), N eam Biers aime Nit ‘ante atic ied cat (yap me / /, f| i Fine @) RIFE mete nine 2-27 Laban 2-29 EF Fa FE Aa BE 9 33 — 1+ AS AB BLE Ee NA Sieh BM — 8 fh — EB HC the helix-turn-helix motif) (i 2! SIE MU HE. EO He AS RR I A RSF SERA ee A A ME AY OR HE Cfour-helix: bundle) BUCY 2-30), Rossmann ii th Fk Rossmann $A&(Rossmann fold) Hl 2~30) EH BY BoB HEE —ite JE RR Baad et SM MESA eTBE RORSOSIMOXK + 63 + zane 9 ttf, sana Men aS wine AE Se (BY 3-26 UA Ab a 9 A He A SE A THR A HE MORES RAN SHRRANTRA COSEREA—H CARR RA MT BEN SUF FRAP AE BK SZ eA HS AE A FF | A a HED OR — 5 Le Mk HA a BS — A EE MAD. PE LIE BURY — Ed Ha SoA Ha eH 5 A PA GAS IE SP. SE EK. RIGA A — RT a La A A AE TM EE FE (BECHER AE AF eT BRA LS RA A BS MKS RAR AE Gf SPAN Be TE AT A SE AACE CTE SZ 9 eH BE a Fh — PR RAR HE | KS TE Kh A RAR AT AB AL OL 8 «A BE A 5 A ‘Re aE I 8 EF TE RE Hy META TE HO LE En» 9 A RE ERR RIE — RIE EO. 15 um BA — 7 AY HE A 20 PRAIRIE 4 FB OL AK BSP OP SSE (2.5 ~3..0 nm), te, Be 20 7 EE aE AK ATOR ASE HRN) EE LB OCT 327) ABCA I a EA I — A Bete. ‘BUR HELE IM Chydropathy plot) Xf Ft 5k — 41> BE 65 0 BEM t+ FT FL» A eK He — HL OR A TE We 9 — 5 A aT. 38458 BEA (carboxylic acid transport sensor) tt 77K HE fF PH CER 8—28) LI LY FCAT 1B EA eS RE SKM. 2 TK PEC) 3~29) A068 HE aA 7 A EZ LE SSL “FR CBRL 330). SEH A IE AB He Fh A «A A BB CS RE 1 — NOS eS A CH Bw — EA EE AY IC, « SE — PE BA BBB A— OM, He 0 HI i SP BAX NR EE OX RAGIN SY EAL BH Ae ty A ah OU He eK A AL A BE A — A UME GB Hh = He OTE OB TY I RE Sy SE (83-31).1 64+ Bm REMNGMS He HE 3-27 AREA ee rman moment aa 30 Too 10300330 300 away 3-28 RRR REE Oa A He EI 1050100150 200 280 Me { z, ae z okt ' 1030 100 180200250 RRS BH 3-20 aU BAR EL Oa A E 3-30 fA BEAR B= 8 HY SE 7S A ALT HAE FL = a RE ‘ESE ANS 3A $5 BEAL OD HE EAE Ze i TLS ESE AA 2 6 RE EB IG A TT 8BES mye + 97 + FORO BD AT DAS FARR HEM Ze: LD HEP ik FS ACR I ‘Re Ae IES] AE MEAL LL. RTM. Koshland il Andrew D. Mesecar 1 SFE #8 2, MR RAT BEE RS BA HEN LORRI. SOE Meé Bt .IDH 7 AEROS D-H ER HS HERA RIL SBS AMES L~ SRAM EL IEA AR TTI THE Os BO OO PERS. RFA eA Fe ID SAAR SF ae SP EO A, Koshland EBB. RA — HE A 5 IER ASH A LAA LEA ASAIN RE A A BIE YT ALMA). FIL, Koshland Al Mesecar UH (R(R= SUI AR AL DL LE — 4 ES A HR. ART. EET FA AE AT HE AR Aa ELE OR RE A RA Sb TE HE SEA HE ee MM EE SB AR REA AT BY ET AE — AB (ic ELBE BE 9 — RSE HS A — AEA, HA A OC Bs — 4 i A 0 GH oy RE — A UA AF RE” Cfour-point landing). M&F te. Koshiland #1 Meseear $i = #02” Be 7 BE 5" DU 2 tic" BLALIML (four-point location model), 4. BLS A ti A DT Be te — A A Ce SEF A I A eR A AE iMG 100 °C CH & ABE 37 CEFF) «101 kPa. pH Hi 7, Se AYR BL A A A EI 55 AR AGF A A LN 5 I ST AERO LA «QU SEiE. pL UR AL I RAS 02 OE REA RR ‘BSH pL EA A Fa RR AT ST BE 6. BBW IY HB A — (Aa Zo A SP meee. 7. PPS METH HE Ae TEM BF Fe Me He AF A A TE BRT AA 9 A MARAT Lh « ad — ff sO OYE MI MIATA LD AER RUE Fa Be ne. ERD anosnes BUA H9 LE A 1 000 BALL OME RED AL 100 AE A A LAF 8 7 WH EE RE ET PREM AMAT. —. MHRK DAS he AE AE AD ty fr % BW Hl (Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, NC-TUBMB) (#8 1 #248 EZ GEAUHEIRE ABIEA OY 6 KES #5-3, 8) a5 OmTR MMR RS-3 BHAARARH x oH Rie = ol ‘HACHE RBH oxidoreductase) 7 BRE Come a BAC AAG CR PUG ra+ 98+ Rom mONSMS IH ee =H eR om BM Carsten) MRE Aim A SCREM AHEM MAL PAE MAE NMRA em eT . AMI Chydrolases) mating Bacio Wea mi TR AEST BSC RC OB RW REByases) IME READE KT BLA A LAE eer Cee aoe 59496 Gaomerases) Emo mew eesti REE 2H SPN EFA) ARM Cigases) AM ATP AF mq ie IRC se ese HEA — ABET 5 RT BAB AS LO PRE SLA ES. Sh Oy JL. 4 a ap SAREONTAS A —TMEL ER UES. GBA WI AW AAALAC Ae. Bi BO PLB St I ECL. 1. 1. 27 SEH EC eR MBE HE BA Se Be Se a 9 KH SERB He ASP 09 98 — ES AUC ARE) CHOTD St a7 98 of 8 28 — AE EAS NAD 9 HA SE AD AE ER POMS, =. Se #LAE NCIUBMB (RED, 8 — MM FAS Fk RE. RRR AA “Yi IR Ae As A eA ER A RL YR — A SY A 9 39 FD I IL RR. NAD BNE ‘OH Zt BEE WR A RA ELAS GBA AR FI Oe 5 TA FRB EL TR SE TE. SK CI HI I PRE ase” > A BCE AFR IX HH BLE pepsin trypsin Al rennin, pi FARA % WH AR HR A FAC RR — BE. RT AK ETE» A 11 2D tO -AE BI A I HR FH BAB DA ATP Gh BAe ok HM AA ATP AAC ARE. AV AE RE (I BA A SBCFE-% FN Se PEAR 5 Me a — blind a — ice a mA QD CA 1. http: //users. ren. com/jkimball, ma, ultranet/BiologyPages/E/Enzymes. html 2 hutp: //www. estrellamountain. edu/faculty/farabee/biobk/BioBookEnzym, htm!be eA cM MANN CRI + 137 + SE HA ST Fb, TP TRE 9 CB 78) 24 Glu A AF RH Eth © RF De» Fe HF TE APRIL eA 1 SY CE aE BE Asp 52 a He MAb WR REAR «A «TE EO HE. Gieas Guess lw3s t 07 Son » AON enon H 0. On A ~ ouB 2 Sy 1, . H-Ft " ie yc omy OG ont Oo Hy _ CH, on Gtuss c. oN ¢H,OH H CH,OH s$ re | 4 ot ° Se7 i Asp52 FB 78 IGN ef FES» RG LST 5 1 7 He DHE I y S1 A oPO, G A OE C C superoxide dis ‘mutase » SOD) 2 Fit 5.55. SOTD 8 HE FAA BB A we A PRIA TA HEL A 11 5 A PR AER | AOS SF AN SF SITE HE PY Cult I Zn", Zn EAE PLB RO Fz fe ACR 7-9), Bi—Cu"* +0; — B—Cu* +0, Bi—Cuv +0 +2H* — Be—Cu"* +H,0, PSE HE HOM) Clul32 Al Glul33 HER ARF 8 Lysl36 WR SAME. SE RR SERA A MSF 5 GH He AE a A 7 Bh — PA BP IEE PW 1 A A COR A) — FACT ELLIO, BRISLEREE «(ELAR ADF HA 8 HS — Mei TL OS A PS ‘EEE CREAR AA EH» FA — AZ 9 (RR BE. I oA AC OC HD+ 132+ =e mes BE HL7-9 BEG SOD M=HE HIN AUR CIS. AAEM AF ES Je AE EP BC «DT EA A (BR) Sm REESE — UG GB AS FE HG ME tH AS, — AE Hs SI BHF Metalloenzymes) — 25 SIR ACE ME (Metal-activated enzymes). HA 8 A We SEH fA de I SF» 2 Ms ME SeI tn Fe™ Fe? \Cut* ,Zné* JM" a CoP «ej 85 FRA eT SF ICS A I a: eI Nat \K* \Mg’* at Ca®* SAR FSS ORCAS MMC. SRB EUS HARSH: D tI Lewis MBH FT. 6 eH LR BSF CA HER D5 0S A 0 TW EUs DA 3 ABE WE AS dy As a AS a A I 5 A © MAH — Ms. BR ERI BE «BAA A AF 1 SC HH SRB REA Pb) Zi AE BEAM FMEA RE CO, FAY C AF FREE HCO; , I 4 mtn —-0-€ | ee Im H o [eno r Va ito + HY + HHO-C { \ Im H o nee (BE) Her hee SY A A AR GE 5 A HM a OF A AE 0 — A A A. HB SAR AR I AN ET HE 3 A A. YS, Lys His Cys Asp, Glu, Ser a Thr, ste Shs — 28BAS MHMMRURAR + 165 + AS UU cm sega 1. http://www, Isbu. ac. uk/biology/enzt 2. hey Zhou G W,Guo J, Huang W et al. Crystal structure of a catalytic antibody with a serine icience. 1994 ,265, 1059-1064 ‘h/engineering. html nology/CHO5/catab. protease active site.