生物笔记introductiontobiochemistry

1、BIO107 Introduction to BiochemistryGuoxia HanLct.1， chemicalQuestionsChemical structure ， interaction ， extract energy ， store and transmit the information changes， controlled3 principle areasStructural Chemistry ，Metabolism ，Storage， transmission ， and expression of genetic informationLct2, Ch03Ami

2、no Acids, Peptides, and ProteinsAmino AcidsCOO- .IH3NC HRIsomersStructural isomers Cis-tra ns isomers En-an tio nmers 性异构体Stereo isomers结构异构体顺反异构体 光学异构体，手空间异构体Ala丙氨酸Stereo isomers 空间异构体(Glycer-aldehyde 甘油醛、tchojMJ TIl jlyc«r4ild«h/d*L-AhnineCHQiH7 -OH roGlycvrjildahydsCQQJH- C NH,To-AJiini

3、rw-蛋白质中出现的氨基酸都是L isomersAmino Acids Classified by R GroupsNonpolar, aliphatic R groupscoo-41coo- 1coo- -Hcoo- 1鹅HHH C HlCH.H2C -一 HjHjN-CH1 CH / CHj CHjGlycineAlanineProlineValineCOO'coo*COO+HjNCH |H C HH,N(1:H曾HCCH,(:h3 iCH/ X 0b C»tCH 3 ch3CHa<:HaLeucineIsokudneMethionine非极性脂肪R基Glycine

4、甘氨酸Gly, GAlanine丙氨酸Ala, AProline脯氨酸Pro, PValine缬氨酸Val, VLeucine亮氨酸Leu, LIsoleucine异亮氨酸Ile, IMethionine甲硫氨酸Met, MPolarz uncharged R groupsCHjOhSeri neCOO-H,N -tHHcOHCHjThreonineCOO"* IMjNCHCHAsparagfnecoo-+Hj N C HCysteine8b* IH3Nc -H严ch2H2N DGlutaminePositively charged R groupstcxrCOO"COO&

5、#39;HjN-C Hch3NH3NHC=NHjHnNCHICHail >CNHLysinenh2ArginineHistidineAromatic Rgroupscoo-HjNc-tiOHPhenylalanineT yrosine1、极性不带电R基Serine丝氨酸Ser, SThreonine苏氨酸Thr, TCysteine半胱氨酸Cys, CAsparagine天冬酰胺Asn, NGlutamine谷氨酰胺Gin, QT ry ptophan非极性氨基酸疏水氨基酸 丙氨酸Ala缬氨酸Vai 色氨酸Trp蛋氨酸Met正电R基Lysine赖氨酸Lys, KArginine精氨酸Ar

6、g, RHistidine组氨酸His, HGuanidino胍基Imidazole咪唑芳香族R基Phenylalainine苯丙氨酸Phe, F,非极性Tyrosine络氨酸Tyr, Y,极性无电Tryptophan色氨酸Trp, W,非极性Indole ring吲哚环8种亮氨酸Leu异亮氨酸lie脯氨酸Pro苯丙氨酸Phe2、极性氨基酸亲水氨基酸：1 极性不带电荷：7种甘氨酸Gly丝氨酸Ser苏氨酸Thr半胱氨酸Cys酪氨酸Tyr天冬酰胺Asn谷氨酰胺GinAla nineAla A non polarNeutral1.8Glyc ineGly G non polarNeutral-0.4

7、Isoleuc ineIle Inon polarNeutral4.5Leuc ineLeuL non polarNeutral3.8Methio nineMet Mnon polarNeutral1.9Phe ny lala ninePheFnon polarNeutral2.8257, 206, 188 0.2, 9.3, 60.0Proli nePro3 non polarNeutral-1.6Tryptopha nTrp W non polarNeutral-0.9280, 2195.6, 47.0Vali neVal V non polarNeutral4.2Histidi neHi

8、s HiPolarpositive(10%)n eutral(90%)-3.22115.9Argi nineArgRPolarPositive-4.5LysineLysKPolarPositive-3.9Asparag ineAsnNPolarNeutral-3.5Cystei neCys CPolarNeutral2.52500.3Glutami neGlnQPolarNeutral-3.5Seri neSerPolarNeutral-0.8Thre onineThr -rPolarNeutral-0.7Tyros ineTyr YPolarNeutral-1.3 :274, 222, 19

9、3 1.4,8.0, 48.0Aspartic acidAspDPolarNegative-3.52 极性带正电荷的氨基酸碱性氨基酸3 极性带负电荷的氨基酸酸性氨基酸3种赖氨酸Lys精氨酸Arg组氨酸His2种 天冬氨酸Asp谷氨酸GluGlutamic acidGluEPolarNegative-3.5Reversible formation of disulfide bond两个半胱氨酸的巯基形成二硫键CjfltcilTMBCysteineAbsorption of ultraviolet light by aromatic amino acids 色氨酸、络氨酸的紫外线吸收图于向

10、5;LanbertBo&r Ljapbnl aJl vail.4-Hydnpcy profiiwS-HydrciBylysincCH, NM Ol±CM 2 CWj CMi- CH COOUncommon amino acids also have important functionsCOO c y| P *OOC C HCHjCHCMI呗ResiduescfesfeoT byo/cow朋ar wsn曲旦用却ofy irruo炉or耳担时 rtrrta?polyp&ptHKSe CH, CHcaaJ*NNtSlenx 艸 *l n</a拦,Mpdi/ce詁 d

11、s祜 fNDi&inrafter ifiarr阪跡a “jtjy你桅刑网伽怖n* SOQaddit io nd anino addshave bean fouhd in cells植物细胞壁胶原质 collagen,胶原质collagen，肌浆球蛋白 myosin， prothrobim，elastin弹性蛋白细胞中还发现了其他300种氨基酸这些残基residue通过调整已经组合成多肽的氨基酸的常见残基而形成Reversible amino acid modifications involved in regulation of protein activity 氨基酸的可逆修饰控制蛋

12、白质的活动-014.-043 -H -CDC "ilMA -OY YU 3-Ml.CH-COO "P P -O-CM -CH-CM0>PultmaW iwlhrl rrtw.-coop口_<1_ 町一 tsFtKMipfKlStrlllffiAmino acids can act as acids and bases 氨基酸的酸碱两性Zwih*fiQrt M pcidFtC ：=C*NH, Zwinafi 口 n tut*I. I 讣十0_2Mln#ri4HifannZwrRtfionH tMfVNon-ionic form 非离子态；Zwitter-ionic

13、 form 两性离子态；Amphoteric 两性的对Gly的titration滴定'NIC.COO*C0HOH13洌031,5OH" (equiva lenti)Isoelectric point (or isoelectric pHpl s 滋的 + pfc?) s % (2.34 + 9.60) 5.97比照Gly滴定与乙酸、甲胺滴定结果Methyl subitituted carkojcyt and amin& graupAcefi-c ocidThw Hrml pKj. lor carlMsjrl group h ibcurKAH4M*Me th y lar

14、nurwT h no rirm I pK for animln£>giiDL»p Is-ibsutlO.t.Orts-orjiiiland dmi no groups in glycine<r-Aminre «td glycirrw 叽 244lluliKon !brtw<eE-n the ahiEriigrayp *nd th? drtiri-9： protwIswflFtfeha pJT. forth-* rirb«Hylgr&up,chAfedrraups kw«f thrstabi-Kring Hie zwiH

15、emwi.ui"Amino odd (glycin«)prR 二 g.«oE：l皀呼a；tl*e> DMyen atd m »In the wfafixyl gmp pwll ttadtram"from lh« dmlno graupr|<Fw«rinj| hs p<p；Amino acids differ in their acid-base propertiesR基do not ionize的氨基酸Ion izable R基的氨基酸三个ionization电离阶段 3个pKa值Peptides are

16、chains of amino acidsH3NCHCOH + HNCHCOOH Rf一y I 11 oAbiihi-terminal «ndCHjCHmiH CMjH CM.J JI I叱十rH o ri oH CH：-ii-im aMjNCH C NCHCOO'TABLE 3-4沁Plohins gnxfpUpcprvtvnsUiMs仿-Lipoprotein of bloodG叭邮慚越n?CflrboMf«iMmunotfatMJlin G.灿山pic：動Pt僧甲阳亞即声C豈飽in of milkrlcrnwrowirtshome ifon p«rp

17、hiinHemogioch钉emj网费wD 耐if, nucieot d«Sutehate'/thllCipFOtJtHflSkORFerittnImcAlcoholCaltiuniClnioduliriIfciytKtantfnIniuogpfiascCopperPlasty i in5Serylcrf ye iltyrosylalanyi leucine or Serly-Tyra-Leu or E&YALHydrolysis & CondensationPeptide bond 肽键 Di-peptide 二肽Penta-peptide 三肽寡肽、低聚肽

18、 oligo-peptide polypeptide 多肽Multi-subu ni t prote ins 有两个或更多的多肽链non covale ntly 结合如果至少有两条链是identical完全一致的-那么这个蛋白质是oligomeric低聚物的， 而这些一样的units包含一个多个链被称为protomers原聚体 自然产生的蛋白质的residues残基通常少于2,000Polypeptides有独特的氨基酸构成一些蛋白质包含不是氨基酸的chemical groupsconjugated proteins并合的蛋白这些非氨基酸的局部通常被称为prosthetic group辅基Pr

19、otein Separation and PurificationColumn Chromatography 色层别离法Crude extract 粗提取Fractionation 分馏Ion-Exchange Chromatography离子交换色层别离Palymef b»d$ with r»egbvcJ> K tUliCtL4H*lgtCi«P40 Net prositivechiarg1 ftiBt negmtivpchdrgp Larg« net ri&itiwe chdrgieBfffti旌： wye &¥U&#

20、187;fl包含负电官能团的聚合物球珠蛋白质混合物与阳离子交换剂参加试管蛋白质下渗的速度由他们在当前ph下的净电量决定。阳离子交换剂使得负净电量高的蛋白质移动更快被更 早洗提elute出来。PtQtelrtrtiiXi(urel$ vddrdto cvl umc conUi ntn-g drtioii Hhonoan.1 13 4 "Protei ni move thro ugh the colurrin di toi » determinesl by fhcirn+t rg|» pH b«ing wtd. Willi cation ecchA»

21、;g4r±F pot«inswtth a more negative net dwge move fasl&rnd elute emFlienExclusion Chromatography (gel filtration)排斥色层别离(胶体别离)Prvteln miirtny h 己<1出乍诂 column con tain inq 匚ra»->linked pal ymr.aPgtein unatecules part by sie- larper n-iolecule? mor色frwljt appearing iflth-e «

22、;arll«r fr«ction多孔渗水的聚合物球蛋白质混合物与cross-linked聚合物参加试管蛋白质分子依据大小不同而被别离更大的分子更容易通过，出现在更早的分馏部分fractionTABLE 3-5 A Purification TabF& for a Hypoetlcal EnzymeIActivity (unitsSpecht acuVify f顾甲媲PfocfiOtjfC of stepFfOCtfOfl VU/urne M1. Crude cellular extractL40010.000100 000102. Pretipjiaiiofi wi

23、lii ammoniuin sulfate2003.00096.00032王Idn-exchange前忖町白g朋hy90400SO .JOT2CO4. Sizf：轨【usicinRDtoo&0 OOC颐s Affinity chromatngjraphy6345 OW15,000Mote: All data represent the 融tug 时 the sample aftw ne ties, gnsted piuceduic hx been earned DuL Activity and specific activity Hie de fiftKi on page 9J.Aff

24、inity Chromatography同类色层别离Pirdlciri al ilVW 討roluliDn*蛋白质混合物蛋白质混合物与结合着配体ligand的聚合物参加试管,配体能够与想要的蛋白质结合杂质蛋白被冲出试管配体热溶液想要的蛋白质被配体溶液洗提岀来U nw«int«d rclvint are wished threuh column.Fnxtcin of Iniamt11 fluted by li<jand wlLtiion.Activity®nits)表示一份溶液中酶的总单位数量Specific activity(u ni ts/mg) 表示每毫

25、克总蛋白质酶的单位量；酶的纯度1.0 unit of enzyme activity = 在25C和最正确测量条件下，每分钟引起1.0 (imol底物转化的酶的数量(amount of enzyme causing the transformation of 1.0 卩 mol of substrate per minute at25 ° under optimal conditions of measurement )E-echophore-s<?$¥箋豈 w po<e醫弋57套CD«Et-x-sB劉 p-oHr心 ptGl® 甯epcoo

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28、There are severa 二 evewof profein sfrucfurePrimarySecondarystructure structureTertiarystructureQuaternarystru ctureAmino acid r«»iduesPolypeptide chainAssembled subunttidtorirtrit £f HilrwKmwul midw 衲itlFCFCOTH尸H占F- s rh -.irT-iS n 海Ufml： mlrigJ wtn kJLfv： |puri> hdWcydH ImdlniHQi皿

29、中也忖祕1前1 Itvcu gh Edm in pkkzke.oiN PhihnybwVtMi t r*lkait»o Helix t1氨基酸残基的线性序列氨基酸残基residues,包括二硫键包括a-螺旋，3 -折叠，3 -转角,2局部稳定的氨基酸残基序列所形成重复出现的结构模型,无规卷曲四种结构3在二级结构根底上进一步折叠成紧密的三维形式多肽链，多种3d折叠后的多肽4由两个或多个多肽链亚基相互作用形成的空间结构。由蛋白质亚基结构形成的多于一条多肽链的蛋白质分子的空间排列组合在一起的 subunit，形成 Multi-subunit Protein , Arrangement is

30、 space of polypeptide sub un its。Determination of amino acid sequenceThe ami no acid seque nces of millio ns of protei ns have bee n determ ined.数百万种蛋白质的氨基酸序列已经被确定Short polypeptides are sequenced using automated proceduresSan ger'method 测定 amino-terminal 残基The Edma n degradati on procedure 降级过程由

31、一个测序仪进行Large proteins must be sequenced in smaller fragment打断 disulfide bondH衣酬皿生Ee=osgCsleR dcld iviMim3shC»H>IO43SH口 iBhriQittlftihtiHfQTTI撕裂Cleaving多肽链TAELE 3-7 Hie Specificity of Some Cam men MisiihiMl& for Ara暫iwntin醴 Polypeptide Chains細砰綁打财q畑1 SNTEerCM卿碑 PCM&1IrjWlnLjfsAnitO(tw

32、ine pencreasjprritnn.WhiriOU!t SU DlTdlil J"ChyDlffpslnPta, rep, tyr (C)Ibnwine!盟 ncira引S 却fl) IMOCCUE 3<jrFLIS V8 prD'B&SPAsp. Gill (CfbactMLini &. aurei/sl'JUp, Gib '4：ibiiiCtwuni 咋畀加治* iPfW.Trp.TyrfN(pofci stiwraen)EndDiifOte 的第 1爲 CLWC>ibaotmuni £ys Dbsc-teref

33、lryoxcger.flsl匚炖 nogfi EmmideMec 临fftl mearti ArtfK(WBR?n hrarwn 締rk厭豔 ii m mMIW IMM AbWWi!l bSuWlliWUMtaniWi£lfti (HlnMiy fficnKW |Mht M H91 RA4WD 即你呪 |1口血ctetMgE ok Ln on eMrirw iwUenwI iC) m IhrmitfurcfcMKl who sao niti亦札一些proteases蛋白酶只撕裂临近特殊氨基酸残基的肽键Ordering the peptide fragmentsProcvJuiire

34、hjMlroljFLB； MfN# ft«PoDypfitiiSei bmI mMi FQNfc hdrsly 胃Xw BtfcllM*dLKV-AwHdtinntis IR turrscnciResult3 H 2 fFTl2, l 心 1 I * Jl1 15 L_1V 11 I it d F 12i -DiniLrQRh-HiyllurUmMKdetKtHiConclusion 啊I邛询I曲h«s-弭 抑疵事ld申藪届x仁Tip fcirt wlH* f l 1* thrM tlnwb 緒1ro*nt 冃 wgii m再 rw? K Lyell lo * wfour

35、hag- HMnti.cy»ii4#a a b* will 館(Mrt) ifr fk« th#w fwpvwit&.E RGilup /miriv- lErnninal rendu e.cM*e whh trips*1- f*p4raM bHmwli iMHiMfd 芒* &drnin H| |*1刑卑，1<!«<* whlif!网*昨 iW*n*«Tf：- EGAftYHU FEFI&PR-1r1Q CCVlt$D TLl-RC<iP«TK.乂 我 £CAA YHOFEPID FRG AS

36、M 心：TKDCVHSD回 AUHTLIACAPM口>:cd at om-no lcmi厂 j s btuufte tt (Mf Im wNfi E 芾 lul; plK«d biwux ri doc s mH end with ntArg|4rK(Lyi)<ijciarl-aps wlrdli-；-and f-4 , nlliD'i rigi K/Th;rn tn b« adefcd.<WW"Tir %目 AftiihcHnninuGCl rboxylKnoirrua G> © us _ ECAAYtltX匕咂鹹躬叩l诂

37、fl I吃些竺UH5 Lb© & ©Amino acid sequences can also be deduced by other methods Amino add sequence 1 protein)Gin -TyrPro-Thr lleTrpi n ir ir Ki Hi iDNA sequence (gene CAGTATCCTACGATTTGGInvestigating proteins with mass spectrometry光谱测定法BW1*2W耳禹阳一弍2'HiEdf.swl-iKVlk4J*lSwrrplc&14>.

38、叩 RlurtionHlgrh*1i!屮MO4MWOwo ij&ooSmall peptides and proteins can be chemically synthesizedSmall peptidesand proteins canbe chemicallysyn thesizedO KT-:可 MHB IC. M WrHWprwpnm*i11 wMh.pr-u4*iE*il亍：r «vwmi airovp Ih '-' rtihArii *HIXL 亠Q_rAHi t 3-R FFpct of Stepwlw rirtd on Overall Yi

39、ddln Fpclde SynttHsh讯比詆3» 11Itw Ifftf jnAwMfrM0«99.兆11fig阴21炯K312»94911390iw1 78?応rrMrWrftfrii BLsnelMMdfb MDHygm山rHi工“t 2* r- JfLct3 Ch4The Three-Dimensional Structure of Proteins蛋白质的con formation构造很大程度上是由 weak in teraction稳固的Protei ns in any of their function al, folded con formati

40、ons are callednative protei ns.蛋白质的结构被记录于the Protein Data Bank (PDB),每一种结构都被唯一的ID标识Protein Architecture -Primary Structurecarbo nyl的氧具有局部负电，而ami no的氮具有局部的正电，这使得两者之间形成a smallelectric dipole 偶极子由于这种现象resonance共鸣，每一个peptide bo nd表现出双键的特征并不能旋转pla narpeptide bond 这形成了一个一个plane小板。这些planes每组共享一个旋转中心CaN-6 C

41、c；-C C-M在polypeptide chain上，每三个键划分一个氨基酸当2 = $= 180时，peptide呈最大伸展的结构，并且所有的peptide groups都位于同一平面上我们约定，当polypeptide处于这种结构时， 2 = 0 = 000 IdigrmJRamachandran plot for L-Ala residues 残基 只有没有或极少有空间冲突的结构才会存在Protein Architecture -Secondary Structure少数几种二级结构是局部稳定的并且广泛存在于蛋白质中。最突出的： a helix 与 3 conformationsa h

42、elixAmino terminus0 arbanHydrogen 。口畤片“ Q Nitrogen groupM?血Th©咅加最 is MtT耐她丿(3-6Cudbox yl terminusUh MndfdImHkAi|>M helixa) 一个右手a helix的球棍模型，显示了链内的 H bondsb) 俯视 a helixc) a helix并不是中空的，中心的原子彼此十分接近d)并不是所有的polypeptides都能形成稳定的a helixAnnin 9 t«rnm>sSide cha ins之间的作用可以使结构更加稳定或不稳定靠近 a helix

43、segme nt末端的 ami no acid residues 的特性同样会影响 helix 的稳定 在两个末端的四个 amino acid residues 没有完全参与至U helix hydrogen bonds 中B conformationBconformation 使得 polypeptide chain 形成了层 B sheetBturns在蛋白质中很常见(a) 0 TurnsType IType II180。的折返，包含四个氨基酸Gly and Pro residues 常常出现在 Bturns 里Gly小巧灵活Pro的cis型在紧密的折返中起到作用般的二级结构具有独特的键角

44、和氨基酸内容Cnirit- haliaHhll>iHnd»d4 Idegiiw.Cofflrflf cxr wconcfjiy t/ucius cw ute 襄觇0 j&y torQC卩蜀*ctenxpyMfaveherlgthiProtein tertiary and quaternary structures用沪貳旳fLysozy m eTertiary structure in eludes long-range aspects of amino acid seque nee1氨基酸残基的线性序列2局部稳定的氨基酸残基序列所形成重复岀现的结构模 型，包括a-螺旋，

45、性折叠，性转角，无规卷曲四种结构3在二级结构根底上进一步折叠成紧密的三维形式4由两个或多个多肽链亚基相互作用形成的空间结 构。由蛋白质亚基结构形成的多于一条多肽链的蛋白质分子的空间排列Quaternary structure includes the three-dimensional arrangement of polypeptide chains inmulti-sub un it prote inFibrous Proteins纤维蛋白：结构、支持、外形、保护Polypeptide cha ins arran ged in long stra nds of sheets a-kerat

46、ina角蛋白KeratinhdixTWd曲鼻 oiled toiltefrsrrote小-“片暑韶 si/perf'twst-edeoi1C-30A出f itwr*心心wFragti lamant |(-S-S-J bortds staM2 折e車w帕嘶ry stmceProtofibril ?巴D JTVT!Tt> 即打卄 i， .*：T:£?删K心?UJ 皿m鼻丹理厶比x-村曲讣百- Collagen胶原质：连接组织、肌腱、软骨、角膜、orga nic matrix of bone(总体上Gly-X-Y, X通常为a Pro, Y经常为 4-Hyp)ab) a ch

47、ain 反复的形成左手旋结构，每 tripeptide seque nce3 residues 一圈c) 3条链扭曲到一起 right-ha nded twistd) 3链collagen的superhelix结构球棍图俯视Collagen fibrils 结构25QriEof collagenmoleculesCo«-$trhti«n£&4DA (64Section of collagtn molceule '/UC h CHhij iflHyhiCwYAmPEW*泄rLjnmidwfIsHnWi* Irw-ImKlffii(Mftfd jaMd

48、v* flfWHnorttwanrCly sidt chai nsr Alj sid«1 chninsStructure of silk fibroin蚕丝蛋白：-一层一层富含 Ala 与 Gly residues 的反向平行 3 shets： Permit close packingand in terlock ing of R groupsAntiparellel. _蒸或电歩牟心& <4层与层之间通过大量的weak in teraction结合在一起，而非像a-keratin的二硫键那样的共价键结合从蜘蛛吐丝器喷出的蚕丝蛋白fibroin链Globular Pro

49、teins结构小巧多变Conforination2rOQO X 5 AaMativform9D0X H A100 X 60A抹香鲸myoglobin肌红球蛋白的结构a) Polypeptide backbone支柱以带状图表现b) 外表轮廓图c) 带状图包含 side chai ns 疏水的 hydrophobic residues Leu Ile Val Prod) 填充图包含所有氨基酸的side cha insThe heme group 亚铁血红素Supersecondary structures (motifs, or simply folds)Particularly stable

50、arran geme nts of several eleme nts of sec on dary structure and the connections betwee n them.ib)Loopp BarrelMotifsT*i|i&WdchMiERlb-onuchaav <1Myvqkiblin 11:53-1Protein motifs are the basis for protein structure classificationAllClassification将蛋白质结构划分为四类或交替3alternate)与segregated)All3在某种程度上是隔

51、离的成散布 interspersed(SCOP)数据库TPipJc-Jil rorinXTinn'i.of ProteinsLeft-hnclrdl can iwcttan brlwrcnjgMrdndii ftfery iw 时The StructuralAll a ; all 3a/ 3 (a 与a +3 ( aRLight-hnridrd(&nnfct|gm between B qtwdsTAftLE IAifproihiute Propwtioii aa NekM 刖诚戶fnn伽Efu曲e in負叱更呼卜 Ch “ n W'piChyfnoifypln (34?

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53、变性结构的丧失将导致功能的丧失cmpb士百 t fvdwi HE* 4n in vliJ C*r* rnon-.-£gl! Ei-MVE V *£EaTi fniirfArtMrro-1 C|CK-LdcHD ,.WDiKcrtttNaliircatruLnircCSS&-Folding for many proteins is facilitated by the action of specialized proteins (chaperones) Qrtaj binda to th« unfM*d or pirtinlly folded prpl*l

54、n Bnd !h»rli 10 DmK DnaJ $llmKjl«Ces ATP )hydlro>ly»if by OwK, DrtK A DP biridlft tightly to vht unfolded prottih.DnaJ>DnaKU<Fifold»idl proteinIo QjroELP«dallrFcldad proteinFolded protein (rkiatlv* <onformAti4>n|ATPbndsto DmaK and th-e prattin dimocijtes.i In hacteriBj the liiiclMtide-eiKluiffrge fact or GrpEE. CoAchaperone proteins DnaK and DnaJChaperonins in