االمتحان النهائي لعام 1122
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1 االمتحان النهائي لعام 1122 Amino Acids : 1- which of the following amino acid is unlikely to be found in an alpha-helix due to its cyclic structure : -phenylalanine -tryptophan -proline -lysine 2- : assuming the oligo-peptied ALPHHELICKS forms one continuous alpha-helix, the carbonyl oxygen of the glutamic acid residue is hydrogen bonded to the amide nitrogen of : -leucine -isoleucine -cysteine -lysin -serine 3- the two amino acid frequently found in reverse turns
2 are : -tyrosin & tryptophan -serine & threonin -glycin & proline -leucine & isoleucin protein structure: 4- The overall folding of a single protein subunit is called : -tertiary structure -primary structure -secondary structure -quaternary structure -all of the above 5- Disulfide bonds are most important in this type of structure : -tertiary structure -primary structure -secondary structure -quaternary structure -all of the above 6- which of the following forces are involved in maintaining the primary structure of protein : -covalent bond
3 -hydrogen bond -ionic bond -hydrophobic bond 7- which of the following best defines a domain : -super-secondary region, often shared by proteins that has aspect function. -repetitive super-secondary structure -double bond layered arrangement formed so that the polar group face the aqueous environment while the nonpolar region are kept away from the aqueous environment - an unfolded region of protein 8- which of the following best describe the motif : -repetitive super secondary structure -common non-repetitive irregularity found in antiparallel beta sheet. -protein conformation with biological affect -group of atoms other than amino acid 9- vitamin c ( ascorbic acid ) prevent survey because : -it's involved in formation the proper beta sheet of collagen -it's involved in metabolism of hemi used in hemoglobin -it encourages the formation of disulfide linkage in collagen
4 -it's unusual amino acid found in primary structure of collagen -it's used to hydroxilate proline in the primary structure of the protein. 10- which one is not an example of super-secondary structure : -the pyrrole ring -the Greek key -the beta meander -the beta barrel 11- protein that aid in the correct and timely folding of other proteins are called : -motifs -chaperone -liposome -cooperative protein purification and separation methods 12- the typical order for the major steps of enzyme Isolation would be from first to last : -homogenization / salt fractionation / electrophories /column chromatography
5 -homogenization / column chromatography / salt /fractionation / electrophories -homogenization / salt fractionation / column/chromatography / electrophories -homogenization / electrophories / salt fractionation /column chromatography 13- which separate on the basis of molecular weight : -gel filtration -affinity chromatography -cation exchange -anion exchange -cation or anion exchange 14- what tends to happen to the percent recovery during a protein purification : -the number usually steadily increase during purification -the number usually steadily decrease during purification -the number usually stays fairly constant -there is no general trend for percent recovery during protein purification 15- which would be best to separate a protein that binds strongly to X substrate : -gel filtration
6 -affinity chromatography -cation exchange -anion exchange -cation or anion exchange 16- elution of protein by means of ph gradient would work best with this type of column : -gel filtration -affinity chromatography -cation exchange -anion exchange -cation or anion exchange 17- in the chromatography the experimental setup always requires : -stationary phase & mobile phase -spectrophotometric detecting device -sample in which components differ in charge -sample in which components differ in polarity 18- the degree of separation in molecular sieve chromatography depend on : -the polarity of the mobile phase the pka of the buffer material in mobile phase the chemical nature of the sieve material -the size of the pores in sieve material
7 19- in the SDS-PAGE method separation takes place on the basis of : -charge only, because all particles have different charges but the same mass -the sieving action of the gel, because all particles have the same charges, but different masses -the sieving action of the gel, because all peptide have approximately the same charge/mass ratio but different masses -the chemical nature of the buffer used as the electrolyte 20- how many bonds would be produced when hemoglobin is subjected to SDS-PAGE : if a protein with the sequence (FEWPRQVDMARINE) is treated with chymotrypsin what will the product be : -F EW PRQVMARINE -FE WPRQVD MARINE -FEWRP QVDMAR INE -FEWPRQVDM ARINE
8 oxygen transporters 22-the structure of myoglobin consist of : -almost entirely of alpha helix -almost entirely of beta sheet -mixture of alpha & beta -of unique secondary motif that is neither alpha helix or beta sheet 23- why does the myoglobin have histidine that prevent both secondary CO from binding perpendicularly to the hemi plan : -this increase myoglobins affinity for O2 - this increase myoglobins affinity for CO2 - this lessees the difference in myoglobins affinity for CO2 versus O2 -this prevents the iron of the hemi from being oxidized 24- in what oxidation state must the iron atom be for hemi to bind O2 : -0, Fe (0) -+1, Fe (I) -+2, Fe (II) -+3, Fe (III)
9 -there is no require oxidation state to use iron 25- which of the following is not a characteristic of hemoglobin : -it contain two different type of subunits -it contain prosthetic group -it's an allosteric enzyme -all of these are true 26- in the bohr effect the binding of oxygen to hemoglobin : -is increased by the presence of Na+. -is increased by the presence of H+/CO2. -is decreased by the presence of H+/CO2. - is unchanged. 27- the affinity of fetal hemoglobin for oxygen : -has not been studied -the same as that of adult hemoglobin - is lower than that of maternal hemoglobin -is higher than that of maternal hemoglobin Enzymes
10 28- how much faster is a reaction with the fastest enzyme than without the catalyst : - about 10 times faster -about 100 times faster -about 1000 times faster -about 100,000 times faster -about times faster 29- if the Y intercept of a line weaver bulk plot = 1.91sec/mmol and the slope= 75.3 L/sec then Km equal : miilimoles per second millimoles per second millimoles per second millimoles per second millimoles per second 30- the value of Vmax changes in : -competitive inhibition -noncompetitive inhibition -both forms of inhibition -neither form of inhibition 31- irreversible inhibitors of enzymatic reactions :
11 -bind to the enzyme only at low temperature -affect only serine side chains -react with the enzyme to produce protein that is not enzymatically active & form which the original enzyme can't be regenerated -bound to the enzyme by the lock-&-key mechanism 32- if the Y-intercept of a line weaver-burk plot = 1.91 second/milimole and the slope = 75.3 L/sec V max equals : miilimoles/second millimoles/second millimoles/second millimoles/second millimoles/second 33- when [S] = Km the velocity of an enzyme catalyzed reaction is about : -0.1*V max -0.2*V max -0.3*V max -0.5*V max
12 -0.9*V max 34- the active site of an enzyme : -remains rigid & doesn't change shape -is found at the centre of globular enzyme -is complementary to the rest of the molecule -contains amino acids without side chains -none of the above is correct 35- CTP is a known inhibitor of ATCase the enzyme that catalyzes the first reaction in the pathway for the synthesis of this compound this is an example of : -irreversible inhibition -feedback inhibition -zymogene inhibition -negative cooperatively **Use this table to answer Q36/37/38/39 ^_^ M N O P Q R which 2 enzymes would be the most likely ones to regulate this pathway is Dedicated to the formation of only
13 one product: -2,4-1,3-1,5-1,2-4,5 37- which 2 enzymes would be the most likely ones to regulate if this pathway is freely reversible and can go both ways : -2,4-1,3-1,5-1,2-4,5 38- the final product R will most likely inhibit which reaction : -1,2-1,3-1,5-2,4-4,5 39- which of the following is not required for enzyme to
14 display cooperative kinetics : -multiple subunits -a value for the Michaels constant,km -allosteric sites which effect the binding of substrate to the active site -ability to display a V max -all of these are characteristic of cooperative enzymes 40- consider the following graph to represent an enzyme that works on its substrate under inhibition & no inhibition, according to this, answer the following three questions : 1))which letter represent the maximal reaction rate of enzyme activity under noncompetitive inhibition?? F 2))which letter represent enzyme activity under no inhibition?? A 3))which letter represent enzyme under competitive inhibition?? B
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