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cell bio midterm 1

BIOL 288

sucrose glucose alpa 1,2 fructose
lactose galactose beta 1,4 glucose
maltose glucose alpha 1,4 glucose
alpha helix inter and intra H bonds. h bonds parellel to axis. r groups point outside 3.6 AA/turn to ensure peptide bonds close enough for H bonds
beta sheet antiparellel more stable, straight h bonds only intra H bonds central carbon at peaks and troughs R groups jut out
what makes up phosphoglycerides small, polar r group, phosphate, glycerol and 2FA
what makes up phosphoceramide small, polar r group, phosphate, sphingosine, and FA
what makes up glycolipid single, uncharged sugar, sphingosine and FA
what makes up sterols cholesterol
what makes up fatty acids phosphate head, glycerol (linker) and hydrocarbon tail
what happens to membrane after TT before: parellel and can rotate/move after: FA chain movement restricted and tightly packed
bacterial KcsA K channel homotetramer, each subunit has two membrane spanning domains (m1 and m2- helices) has pore region (forms selectivity filter) GYGVT
euk voltage-sensing K channel homotetramer, 6 helices. helices 1-4 are voltage sensing. S4 has pos (Glu, Arg) pore domain is helices 5 & 6 pore is GYGV/IT
compare euk and bacterial k channels both homotetramers (euk has 6 helices, not 2). euk is a true voltage gated, bacterial is pH mediated. euk has cytoplasmic domain, bacterial doesn't.
how does K+ move through bacterial selectivity filter 1,3 and 2,4 move two in filter at a time. energetically favourable to move through, stabilized by oxygen ring.
how does gate open and close? (bacterial) pH-mediated m2, glutamine gets protonated as H+ increases due to dec in pH. this causes the GLu to repel positively charged ARgininge which it had H bond with. open at glycine hinge
what are GLUT transporters 12 transmembrane proteins. tissue specific. 1-3 are insulin independent and 4 is dependent. 5 fructose dependent
what kind of transport is GLUT 1 facilitated diffusion
what are the steps in GLUT 1 transport glucose binds to transporter from outside, conformational change, transporter opens to inside, glucose released (gets phosphorylated into glucose-6-phosphate), transporter returns to original state
what is/kind of transporter Na+/K+ ATPase pump direct active maintains resting mp, creates a steep ion gradient that is important for indirect transport, maintains cell volume and resting mp)
steps Na+/K+ ATPase 3Na+ bind from inside cell, ATP phosphorlyates pump, conf change release Na+ to outside, 2K+ bind from outside, de-phosphorylates, releases K+ inside and returns to intial
what is the initial state Na+/K+ faces inside
what is Na+/glucose symporter type of transport indirect active
what is Na+/glucose symporter steps binds 2Na+ from outside, glucose binds soon after, conf change, symporter opens to inside, Na+ released to inside (soon pumped out byNa/K+ atpase. glucose released too. empty symporter returns to initial
what is the intial state of Na/glucose open to outside
what causes cystic fibrosis phenylalanine deletion in the first ATP binding site (that drive Cl- tansport) Cl- cannot pass, neither can water or Na+
what is cystic fibrosis transporter 2 transmembrane domains for Cl- pore 2 ATP binding sites drive Cl- transport cytoplamic domain
what kind of transport is cystic active
what are the basic properties of cells life, highly organized, genetic program, produce more cells, use/acquire energy, carry out chemical rxns, engage mechanical activity, respond to stimuli, self-regulate, evolve
what is the significance of van der waals and hydrophobic forces weak individually, but collectively strong. universal, allow for protein shape/conformation,stable DNA strands when separated and bind'/interact btwn proteins and molecules (ES complex)
properties of water cohesive, temp stabilizing capacity, solvent properties, hydrophobic effect and acid-base chem
what cohesiveness due to h-bond network
what temp stab capacity due to H-bond network
what solvent properties due to polarity (hydration spheres)
what hydrophobic due to cohesivenss
what is quinary structure of proteins non-covalent interaction between molecules that organize the cellular interior. structural elements of the cell. substrate channelling
what is substrate channeling when multiple protons (metabolon) work together to move a substrate from one active site to the next seamlessly in an ordered fashion to speed up reactions. like finding friend in bar
what are the membrane functions boundary and permeability barrier, organization and localization of function, transport processes, signal detection, cell to cell communication
what are the three classes of proteins integral, peripheral and lipid-anchored
what is abundant on the outer layer of the membrane sphingomyelin, phosphatidylcholine, glycoproteins/lipids, some monotopic/peripheral proteins
how membrane asymmetrical in ER-Golgi-sent to PM. in ER(adds phopholipids, scramblase makes symmetrical. in golgi(flippase makes the proper proteins on each side-assym)
what are the factors affecting transition temperature of the membrane degree of saturation, fatty acid chain length, and sterols(cholesterol)
what are the enzymes that remodel membranes to keep them fluid a) desaturase enzymes to convert single bonds to double bonds and move with kinks. b)shuffling of fatty acyls chains-phospholipases (cut off chain)and acyltrandferases(move other chain into cleaved)
what are the 4 types of transport ATPases P-class pumps, V-class proton pumps, F-class proton pumps, ABC superfamily
what is P-class pumps reversible, phosphorylated by ATP. 8-10 transmemb protein, transport cations. sensitive to vandate (vo43-).eg=NA+/K+ and H+/K+ ATPases
what is V-class proton pumps on vacuole/lysozymes. 2 multisubunit components, v1- peripheral cytoplasmic component that gets phosphorylated by ATP
what is F-class proton pumps "factor", inner mito memb and chloroplast. 2 multisubunit components. f1-peripheral. protons move down conc grad. ATP binding site, can synthesize it via ATPase via proton movement b/c proton pore moves w/ grad. can pump other dir using ATP BIDIRECTIONAL
what is ABC superfamily 150 transporters. ATP binding cassette. 4 proton domains. 2 integral(t)-hydrophobic,6 transmemb, form channel. 2 peripheral(a)-bind ATP. heterotetramer. move ion, sugars, AA. medically relevant.
what are the steps in citric acid cycle (substrate channeling) L-malate--mMDH--> oxaloacetate--CS-->citrate--ACON-->isocitrate
Created by: abc273
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