worksheet2AK - MCB 130 Sections 101 and 102 Week 2 Membrane...

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Unformatted text preview: MCB 130 Sections 101 and 102 Week 2 - Membrane Transport Proteins GSI: Jackie Chretien jacquelineaanberkeley. edu i. What is "hydropathy anaiysis" and how is it used? Camphdtcdhflmal anahssi s u{ M HA" Pk‘flo" C‘h'j 0‘i A («3va Lusu Alb-3 in +w\¢\&uwc“ ode Kit 1.1544 +0 git-(Amt W/wkdrw A fwd-Lin mu] tot-crack aux—HA MLMMMM. 2. How are the structures of porins different from the structures of most transmembrane proteins? 'iPM as barn an“: 43 \ A 1‘ “ad-0L bail-rd s “ M3- Ao nu+ hurt “anti-r 'c-njr ska-ms o€ ufiwwbtc residues. M tut-wad uni/MM. Wm vio- “\mmha) “meme {k-smembtc my“; {.4 M} Y:- S‘W-c—ts- 3‘ Proteoiytic mapping lane A: untreated 1 lane 8: trypsin added to intact Cells 2 lane C: trypsin added to fragmented ceiis Draw proteins 1—4 in the membrane: 3 4 At \cd ‘qu-f M 32C we on cwtw’rl'fiifwa m B M235 \ mgr-9505C- me. MW bflhflfifi { mag-ml , Lfl‘fa . 4. Describe the experiment you would use to show whether a specific protein is motile within the membrane. How would you adapt this to determine whether its mobility depends on another protein {e.g., spectrin)? "Ta-3 44M. erotu'n w'v’rin a-FP or at £lmsmtfi cm-svskkgl Mbbdu$, u“. gage; imbue; Mask-t £1: ekohbuacln one. porth of 4A4. PUFer sawwa. Ly. \Ncyuk- {.4 0L mm a _ 9“ @ W 7 @ \oaupkfimuncl 3m a; mum:- meow-n3 ts 41.31;). ioLuLAv-t rec-arr. M Sam u'n 4b.; qbuna of M Fcku‘q. 5. Name three sources of energy that a membrane transport protein can use. AW or umfi‘“ (155T? afl‘CVV’ma-hbu‘ mam “one, monuies' Ht.) (Jeri-rte fame-Q . [Mi-35* $0911 “glck‘adzmwdealqgradicni' +1: \91: onech 6. In the Na+/K+ transporter, which conformation (i.e., binding site facing cytosoi or extraceiiular space) has a higher affinity for Na+ ions? K+ ions? Why is this important? ashso\ has. mam 94—69%“ Gui” Had I oL‘rraAdL has may.“— fit afiéxidbj. W‘s if: \Mpoflrmt became: it (a Mus-5M3 '5‘» Mai +1: btnd o». M wbtueoh'c. 9am. tow-\— be. when; on M “WC-Luukw fl?an v‘g M was AEWJT “change, LOOBL\A “0"? “CIA/U" dficréhflj. m 6W affindequ rs m ’9; \L‘i \o\¢.\d\i’\cj (loud \in up?0$\-R difzflfli'fi MCB 130 Sections 101 and 102 Week 2 - Membrane Transport Proteins GSl: Jackie Chretien jacqualineam®berkeley.edu 7. Fill out the grid of transport proteins: sedim/ “We in establish-es M'l' +455 ' 3 Na+ 2 K+ o . wk film ATP fl :— 2? l’f- ..-=J - Ca++/Na+ Law; I . We [get] “SMIer In.» t f - H I '3’ “a $in ’5 P“ "‘1 m“ Mr r» Wm WM glucose LW 3 ,r ' ‘ _ / Shimmer m Wm" H“ “"t Wm M “ a porin . “HA \ n/a “M “MM finder? ’ — lactose UM“ _ w I gig—Hulk; lat,ch as permease ad'we’ Hf i “ll M. “ latch in mum Shara. Gar OJ 8. Draw a diagram of the basic steps of histidine transport. Label all relevant cell structures and proteins. O“ IN iM H'isl’ h 493135 film a Aw ATP 5 G) p E ——5———» Q *wshaim W5 M H ADP . u - ms‘ndiw. is lanwwl hishclww m5 Risa” M en . Luke: «4. WI 9mm W53 was am arshgm We‘dde 4». erUL HxspQM cpN-QULK 0di— ‘HM. ‘mmx mm 9. What would happen to lactose import in E. coli if you acidified the cell interior? This would disc‘uflr M H* grader,th +6.0er 4% \kc’rosvc Sng M N, \Mlmgg 1W Md ocw. 10Describe how you would show whether a protein is (able to be) transported into the nucleus. How would you determine which portion of the protein is reguired 1for nuclear Iocalizatjon? How would you show that this portion is sufiicient for nuclear localization? LAW “'l'lm gin-Olen lfifi: (2?? V3, ahl’lbéla , gold park‘de3 MA mucosa W5 lowil'w‘l‘im“ Llisw’ Momscz'gxs w 6M) a-H-cr in‘sedncm HMO 0. £05 coast-e... :19"- tha \ a l . -_ 3E @ .v q Mud-xiii reed“. 1's - lag-L‘- fiufl c “a, 85' s . Mull-Ml" I”? mgq‘flj {fir \Mfor'l‘ \ ; Luci squid?) 5w4fi[email protected]:mflq adnim \l/ , 15 ‘m MM) aMmfll “.5, “WW” *@ ‘3 whom a F ' vuers‘rLMI‘M“W' fl”, weary 09W, 5 rue ...
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