1. The B-dna structure found in solution is a a right-handed double helix of antiparallel chains (11 bp/turn) B left-handed double helix of antiparallel chains (10 bp/turn) C right-handed double helix of antiparallel chains(10 bp/turn). D left-handed zig-zag helix of antiparallel chains(12 bp/turn) E right-handed double helix of parallel chains(10 bp/turn) 2. dna differs from rna in the following features a DNA is resistant to base catalyzed hydrolysis; Rna is hydrolyzed by oh b dNA residues are linked by 3 -->5 phospho lester bonds RNA is 2 -->5 linked c DNA has deoxyribose residues; RNA has ribose residues D DNA contains the a.c. g and t bases Rna contains a c.g. and u e All but the second choice are correct d ifferences 3. Because DNa is a highly charged polyanion, its stability to heat denaturation ("melting") a does not depend on hydrophobic interactions B c decreases with increasing [salt d is independent ofG +C content E increases with increasing pH 4. The total contour length of dna in a human cell is about b 1 mm C10 d 1 meter E 12 furlongs 5. Polyacrylamide and agarose gel electrophoresis separate nucleic acids based primarily on their a length B ratio of mass/charge C (G+C)(A+T)content. D organismal origi E content of N (buoyant density) 6. The number of supercoils in a covalently-closed, circular DNA can only be a at least one of the phospho ester chains is cleaved b both of the phosphodiester chains are cleaved c histones are bound to the dna d the salt concentration is increased >10 M
1. The B-DNA structure found in solution is a A right-handed double helix of antiparallel chains (11 bp/turn). B left-handed double helix of antiparallel chains (~10 bp/turn). C right-handed double helix of antiparallel chains (~10 bp/turn). D left-handed zig-zag helix of antiparallel chains (12 bp/turn). E right-handed double helix of parallel chains (~10 bp/turn). 2. DNA differs from RNA in the following features A DNA is resistant to base catalyzed hydrolysis; RNA is hydrolyzed by OH- . B DNA residues are linked by 3'-->5' phosphodiester bonds; RNA is 2'-->5' linked. C DNA has deoxyribose residues; RNA has ribose residues. D DNA contains the A, C, G and T bases; RNA contains A, C, G, and U. E All but the second choice are correct differences. 3. Because DNA is a highly charged polyanion, its stability to heat denaturation ("melting"): A does not depend on hydrophobic interactions. B increases with increasing [salt]. C decreases with increasing [salt]. D is independent of G + C content. E increases with increasing pH. 4. The total contour length of DNA in a human cell is about A 1 mm. B 1 mm. C 10 cm. D 1 meter. E 12 furlongs. 5. Polyacrylamide and agarose gel electrophoresis separate nucleic acids based primarily on their A length. B ratio of mass/charge. C (G+C)/(A+T) content. D organismal origin. E content of 15N (buoyant density). 6. The number of supercoils in a covalently-closed, circular DNA can only be changed if A at least one of the phosphodiester chains is cleaved. B both of the phosphodiester chains are cleaved. C histones are bound to the DNA. D the salt concentration is increased >1.0 M
E chemical reagents react with the backbone phosphates 7. Thymidine a is equal to the adenosine concentration in double-stranded DNA b is replaced by Uracil in RNA c normally forms 2 hydrogen bonds with adenosine D can participate in hydrophobic interactions due to its methyl group E All of the above are correct 8. The major and minor grooves of B-form DNA correspond to what features of A-form rNA? a minor and major grooves b deep and shallow grooves D phosphoribose backbones E Choices a) and d)are both correct 9. The glycosid ic bonds in DNA and rna A be hydrolyzed by o b are free to rotate over about 180 c are restricted to one of four possible orientations E stabilize Watson-Crick H-bonds 10. In solution, the grooves of nucleic acid helices a are filled with H2O and counterions(M*& m2t) B expose the H-bonding groups of the bases c expose the hydrophobic surfaces of the bases D are about equal in width E Choices a) and b)are both correct 11. When an aromatic molecule intercalates into the dna double helix the two adjacent base pairs are separated by about and the helix is unwound by about A342,36° B4.3?,36° C3.4?.26° D4.3?,26 E1.7?,10° 12. If your genomic DNA could be typed for a specific genetic defect a "I would not want to be tested ever b "I would want to be tested now C I might want to be tested later
E chemical reagents react with the backbone phosphates. 7. Thymidine A is equal to the adenosine concentration in double-stranded DNA. B is replaced by Uracil in RNA. C normally forms 2 hydrogen bonds with adenosine. D can participate in hydrophobic interactions due to its methyl group. E All of the above are correct. 8. The major and minor grooves of B-form DNA correspond to what features of A-form RNA? A minor and major grooves B deep and shallow grooves C deoxyribose backbones D phosphoribose backbones E Choices a) and d) are both correct. 9. The glycosidic bonds in DNA and RNA A can be hydrolyzed by OH- . B are free to rotate over about 180°. C are restricted to one of four possible orientations. D connect the sugar to the base. E stabilize Watson-Crick H-bonds. 10. In solution, the grooves of nucleic acid helices A are filled with H2O and counterions (M+ & M2+). B expose the H-bonding groups of the bases. C expose the hydrophobic surfaces of the bases. D are about equal in width. E Choices a) and b) are both correct. 11. When an aromatic molecule intercalates into the DNA double helix, the two adjacent base pairs are separated by about ______, and the helix is unwound by about _______. A 3.4?, 36° B 4.3?, 36° C 3.4?, 26° D 4.3?, 26° E 1.7?, 10° 12. If your genomic DNA could be typed for a specific genetic defect A "I would not want to be tested, ever." B "I would want to be tested now." C "I might want to be tested later
D I need much more information before decid ing E All four decisions are now being made by reasonable people ※<2 1. The a-amino acids have a carboxyl group with a pK around and an amino group with a pK near A1.and12.1 B6.5,and8.0. C3.and10.5 D9.0,and2.5 E 2.2 and 9.5 2. Which pair of amino acids absorbs the most UV light at 280 nm? a Thr h B Trp Tvr. C Cys Asp d Phe pro e None of the above 3. Which of the following is not a sensible grouping of amino acids based on their polarity properties? Ala Leu and val B Arg, His, and Lys C Phe, Trp, and Tyr D Asp, Ile, and Pro E Asn. Ser and Thr 4. The isoelectric point of an amino acid is defined as a the ph where the molecule carries no net electric charge. b the ph where the carboxyl group is uncharged c the pH where the amino group is uncharged d the ph of maximum electrolytic mobility E -logio(pKi+ pKj 5. When the amino acid alanine(the R-group is:-CH3)is added to a solution with a pH of7.3, alanine becomes A B C D an Isotope e an anion
D "I need much more information before deciding." E All four decisions are now being made by reasonable people. 5 ※ 1. The a-amino acids have a carboxyl group with a pK around ___ , and an amino group with a pK near ___. A 1, and 12.1 B 6.5, and 8.0. C 3, and 10.5. D 9.0, and 2.5. E 2.2 and 9.5. 2. Which pair of amino acids absorbs the most UV light at 280 nm? A Thr & His. B Trp & Tyr. C Cys & Asp. D Phe & Pro. E None of the above. 3. Which of the following is not a sensible grouping of amino acids based on their polarity properties? A Ala, Leu, and Val. B Arg, His, and Lys. C Phe, Trp, and Tyr. D Asp, Ile, and Pro. E Asn, Ser, and Thr. 4. The isoelectric point of an amino acid is defined as A the pH where the molecule carries no net electric charge. B the pH where the carboxyl group is uncharged. C the pH where the amino group is uncharged. D the pH of maximum electrolytic mobility. E -log10(pKi + pKj) 5. When the amino acid alanine (the R-group is: -CH3) is added to a solution with a pH of 7.3, alanine becomes: A a cation. B nonpolar. C a zwitterion. D an isotope. E an anion
6. Aspartic acid is similar to glutamic acid in the same way that a His is similar to pro b Ser is similar to Cys c GIn is similar to asn d Asn is similar to gin e Gly is similar to val 7. Alanine is similar to serine in the same way that a val is similar to Thr b Phe is similar to Tyr c Phe is similar to Trp d Ser is similar to Thr E Trp is similar to Pro 8. Glycine is similar to valine in the same way that a Ala is similar to leu b Thr is similar to met C Ala is similar to lle D Arg is similar to Lys e None of the above are valid similarities 9. A significant difference between His and Pro is that a the His side chain is aromatic, the pro side chain is aliphatIc b His is an a-amino acid Pro is an imino acid c the His side chain has a six-membered ring; Pro has a five-membered ring d the His side chain has a pK around ph=7; the pro side chain does not e All but the third choice are significant d ifferences 10. A significant difference between Phe and Tyr is that a the Phe side chain is aromatic, the Tyr side chain is aliphatic B Tyr is an a-amino acid; Phe is an imino acid c the Tyr side chain has an -OH group: the Phe side chain does not. d the Tyr side chain has a pK around pH=7; the Phe side chain does not e All but the third choice are significant differences ※ 1. The peptide bond in proteins a planar, but rotates to three preferred dihedral angles B nonpolar, but rotates to three preferred dihedral angles C nonpolar, and fixed in a trans conformation planar and usually found in a trans conformation. E not cleavable by hydrolysis
6. Aspartic acid is similar to glutamic acid in the same way that A His is similar to Pro. B Ser is similar to Cys. C Gln is similar to Asn. D Asn is similar to Gln. E Gly is similar to Val. 7. Alanine is similar to serine in the same way that A Val is similar to Thr. B Phe is similar to Tyr. C Phe is similar to Trp. D Ser is similar to Thr. E Trp is similar to Pro. 8. Glycine is similar to valine in the same way that A Ala is similar to Leu. B Thr is similar to Met. C Ala is similar to Ile. D Arg is similar to Lys. E None of the above are valid similarities. 9. A significant difference between His and Pro is that A the His side chain is aromatic, the Pro side chain is aliphatic. B His is an a-amino acid; Pro is an imino acid. C the His side chain has a six-membered ring; Pro has a five-membered ring. D the His side chain has a pK around pH = 7; the Pro side chain does not. E All but the third choice are significant differences. 10. A significant difference between Phe and Tyr is that A the Phe side chain is aromatic, the Tyr side chain is aliphatic. B Tyr is an a-amino acid; Phe is an imino acid. C the Tyr side chain has an -OH group; the Phe side chain does not. D the Tyr side chain has a pK around pH = 7; the Phe side chain does not. E All but the third choice are significant differences. 5 ※ 1. The peptide bond in proteins is A planar, but rotates to three preferred dihedral angles. B nonpolar, but rotates to three preferred dihedral angles. C nonpolar, and fixed in a trans conformation. D planar, and usually found in a trans conformation. E not cleavable by hydrolysis
2. The molecular formula for glycine is C2HsO2N. What would be the molecular formula for a linear oligomer made by linking ten glycine molecules together by condensation synthesis? A C20H5oO20N, B CoH3 OuN C C20H4OOIoN e None of the above 3. The resonance structures that can be drawn for the peptide bond indicate that the peptide bond a still isn 't completely understood by chemists B is stronger than an ordinary single bond c has partial double bond character d actually extends to the a-carbon e The second and third choices are both correct 4. The peptide hormone involved in controlling blood pressure is a testosterone b oxytocin d interferon B E glutathione 5. Aspartame, the synthetic sweetener(a k a NutraSweet ), is A b also secreted by the posterior pituitary gland in response to thirst c a glucose derivative D not digested (i.e. hydrolyzed) by humans is nearly 10,000-fold sweeter than sucrose, by weight ※ 1. The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide(CnBr) to produce a Val-Lys Glu-Met-Ser Trp-Arg-Ala B Val-Lys-Glu-Met-Ser-Trp Arg-Ala c Val-Lys-Glu-Met D Val-Lys-Glu Met-Ser-Trp-Arg-Ala E Val-Lys-Glu-Met-Ser Trp-Arg-Ala 2. The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with
2. The molecular formula for glycine is C2H5O2N. What would be the molecular formula for a linear oligomer made by linking ten glycine molecules together by condensation synthesis? A C20H50O20N10. B C20H32O11N10. C C20H40O10N10. D C20H68O29N10. E None of the above. 3. The resonance structures that can be drawn for the peptide bond indicate that the peptide bond A still isn't completely understood by chemists. B is stronger than an ordinary single bond. C has partial double bond character. D actually extends to the a-carbon. E The second and third choices are both correct. 4. The peptide hormone involved in controlling blood pressure is: A testosterone. B oxytocin. C vasopressin. D interferon B. E glutathione. 5. Aspartame, the synthetic sweetener (a.k.a. NutraSweet), is A a dipeptide. B also secreted by the posterior pituitary gland in response to thirst. C a glucose derivative. D not digested (i.e. hydrolyzed) by humans. E is nearly 10,000-fold sweeter than sucrose, by weight. 5 ※ 1. The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce A Val-Lys + Glu-Met-Ser + Trp-Arg-Ala. B Val-Lys-Glu-Met-Ser-Trp + Arg-Ala. C Val-Lys-Glu-Met + Ser-Trp-Arg-Ala. D Val-Lys-Glu + Met-Ser-Trp-Arg-Ala. E Val-Lys-Glu-Met-Ser + Trp-Arg-Ala. 2. The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with
chymotrypsin to produce a Val-Ly Glu-Met-Ser Trp-Arg-Ala B Val-LYs-Glu-Met-Ser -Tr C Val-Lys-Glu-Met-Ser Trp-Arg-Ala d Val-LyS-Glu Met-Ser-Trp-Arg-Ala E Val-Lys-Glu-Met Ser-Trp-Arg-Ala 3. Hydrogen bonds in a-helices are a more numerous than van der Waals interactions B not present at Phe residues C analogous to the steps in a spiral staircase D roughly parallel to the helix axis E about 5? in length 4. In b-pleated sheet structures a neighboring chains lie in a flat plane B neighboring residues are hydrogen bonded c neighboring chains are connected by a- helic D neighboring residues have F& Y angles of about 90o E neighboring chains are hydrogen bonded. 5. If the F and Y angles of each peptide unit in a protein are known, the following will also be determined a complete secondary structure. B complete tertiary structure mplete quaternary structure d thermodynamic stability e Both the first and the second choices are correct ※ Which of the following is an example of tertiary structure in a protein? a polyalanine b a multimeric protei c an a-helix d a b-pleated sheet e a globular domain 2. An"oil drop with a polar coat"is a metaphor referring to the three dimensional structure of a fibrous proteins collagen globular proteins
chymotrypsin to produce: A Val-Lys + Glu-Met-Ser + Trp-Arg-Ala. B Val-Lys-Glu-Met-Ser-Trp + Arg-Ala. C Val-Lys-Glu-Met-Ser + Trp-Arg-Ala. D Val-Lys-Glu + Met-Ser-Trp-Arg-Ala. E Val-Lys-Glu-Met + Ser-Trp-Arg-Ala. 3. Hydrogen bonds in a-helices are A more numerous than Van der Waals interactions. B not present at Phe residues. C analogous to the steps in a spiral staircase. D roughly parallel to the helix axis. E about 5? in length. 4. In b-pleated sheet structures A neighboring chains lie in a flat plane. B neighboring residues are hydrogen bonded. C neighboring chains are connected by a-helices. D neighboring residues have F & Y angles of about 90°. E neighboring chains are hydrogen bonded. 5. If the F and Y angles of each peptide unit in a protein are known, the following will also be determined: A complete secondary structure. B complete tertiary structure. C complete quaternary structure. D thermodynamic stability. E Both the first and the second choices are correct. 5 ※ 1. Which of the following is an example of tertiary structure in a protein? A polyalanine. B a multimeric protein. C an a-helix. D a b-pleated sheet. E a globular domain. 2. An "oil drop with a polar coat" is a metaphor referring to the three dimensional structure of: A fibrous proteins. B collagen. C globular proteins
D silk protein e The first and the second choice are both correct 3. The portion of proteins having the highest mobility are a a-helices C peptide bonds. d surface side chains E aliphatic groups 4. Which of the following is most correct a Charged amino acids are never buried in the interior of a protein b Charged amino acids are seldom buried in the interior of a protein c All hydrophobic amino acids are buried when a protein folds d Tyrosine is only found in the interior of proteins e Glycine is rarely found in proteins because it is too destabilizing 5. Disulfide bonds most often stabilize the native structure of a extracellular proteins. b dimeric proteins c hydrophobic proteins D intracellular proteins E multisubunit proteins 6. Buried hydrophobic sidechains in a globular protein fit into a"hole"formed by the sidechains of a 1-3 other amino acid b precisely six other amino acids C 5-7 othe d 9-12 other amino acids E 13-15 other amino acids 7. The most important parameter relating to the energy of a H-bond in protein structure is: a whether it is found in an a-helix or a b-sheet b the angle between donor and accepter, i.e. 1800 +/-20 c the distance between donor and accepter i e. <3.2? D the peptide bond dipole, i.e.-370 D e the planarity of the peptide bond 8. All other things being equal, the free energy of favorable electrostatic interaction between two charges separated by 4?(-4kJ/mol) will a decrease 2-fold at 2? separation. b decrease 4-fold at 2? separation
D silk protein. E The first and the second choice are both correct. 3. The portion of proteins having the highest mobility are A a-helices. B b-sheets. C peptide bonds. D surface side chains. E aliphatic groups. 4. Which of the following is most correct: A Charged amino acids are never buried in the interior of a protein. B Charged amino acids are seldom buried in the interior of a protein. C All hydrophobic amino acids are buried when a protein folds. D Tyrosine is only found in the interior of proteins. E Glycine is rarely found in proteins because it is too destabilizing. 5. Disulfide bonds most often stabilize the native structure of: A extracellular proteins. B dimeric proteins. C hydrophobic proteins. D intracellular proteins. E multisubunit proteins. 6. Buried hydrophobic sidechains in a globular protein fit into a "hole" formed by the sidechains of A 1-3 other amino acids. B precisely six other amino acids. C 5-7 other amino acids. D 9-12 other amino acids. E 13-15 other amino acids. 7. The most important parameter relating to the energy of a H-bond in protein structure is: A whether it is found in an a-helix or a b-sheet. B the angle between donor and accepter, i.e. 180° +/- 20°. C the distance between donor and accepter, i.e. <3.2?. D the peptide bond dipole, i.e. - 3.70 D. E the planarity of the peptide bond. 8. All other things being equal, the free energy of favorable electrostatic interaction between two charges separated by 4? (-4kJ/mol) will A decrease 2-fold at 2? separation. B decrease 4-fold at 2? separation
C remain about the same D increase 2-fold at E increase 4-fold at 2? separation 9. Attractive van der Waals forces occur a between apolar molecules in the liquid state c between polar molecules in the solid state d only if other forces are less favorable e only in the gas ph 10. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein a only at the ends of a-helices b only at the turns connecting b-strands d about once or twice/protein e only very rarely 11. All other things being equal, the free energy of an unfavorable electrostatic interaction between two charges separated by water(e=80)will a decrease 20-fold in benzene(e= 4) b decrease 400-fold in benzene C remain about the same d increase 20-fold in benzene E increase 400-fold in benzene ※<6 The strong conclusion from anfinsen's work on rnasea was that a 100%enzyme activity corresponds to the native conformation B disulfide bonds(s-s)in proteins can be reduced in vitro C Cys-sH groups are not found in vivo d the native conformation of a protein is adopted spontaneously. E irreversible denaturation of proteins violates the Thermody Hypothesis 2. Treatment of RNase A with 8M urea, but without add ing mercaptoethanol would a not have unfolded the protein B have simplified the experimental analysis c also denature the enzyme d have caused irreversible denaturation e also result in formation of Cys-SH residues
C remain about the same. D increase 2-fold at 2? separation. E increase 4-fold at 2? separation. 9. Attractive van der Waals forces occur A between apolar molecules in the liquid state. B between any pair of nearby atoms. C between polar molecules in the solid state. D only if other forces are less favorable. E only in the gas phase. 10. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein A only at the ends of a-helices. B only at the turns connecting b-strands. C only on Pro residues. D about once or twice/protein. E only very rarely. 11. All other things being equal, the free energy of an unfavorable electrostatic interaction between two charges separated by water (e = 80) will A decrease 20-fold in benzene (e = 4). B decrease 400-fold in benzene. C remain about the same. D increase 20-fold in benzene. E increase 400-fold in benzene. 5 ※ 1. The strong conclusion from Anfinsen's work on RNaseA was that: A 100% enzyme activity corresponds to the native conformation. B disulfide bonds (S-S) in proteins can be reduced in vitro. C Cys-SH groups are not found in vivo. D the native conformation of a protein is adopted spontaneously. E irreversible denaturation of proteins violates the "Thermodynamic Hypothesis". 2. Treatment of RNaseA with 8M urea, but without adding mercaptoethanol would A not have unfolded the protein. B have simplified the experimental analysis. C also denature the enzyme. D have caused irreversible denaturation. E also result in formation of Cys-SH residues
3. If Anfinsen had not determined the location of the s-s bonds in renatured rnasea his result of >90% recovery of enzyme activity would a have proven his hypothesis b not have been believed c not have been possible d have been hard to believe e have gone unnoticed 4. The statement(from Campbell, p 127)that"the amino acid sequence of a protein contains all of the information required for the complete three dimensional structure a cannot be falsified by experiment; hence it is trivial B is strongly supported by denaturation-renaturation experiments C is called an"hypothesis"since its valid ity is sort of dicey D is called a"model"because it can be diagrammed in textbooks e has essentially been proven by recent theoretical work 5. Anfinsen probably chose RNase A for his experiments instead of say, trypsin or chymotrypsin, because a trypsin would digest itself to oligopeptides under mildly denaturing. conditions(slow removal of urea). b RNase A is less expensive than trypsin or chymotrypsin C Trypsin and chymotrypsin are intracellular enzymes(no S-s bonds) d RNase a has only 25 amino acid residues e RNase a does not have any interfering His residues 6. Which of the following occurred when RNase A refolded? a The primary structure of the protein was rearranged b Most of the charged residues were found buried in the protein C The entropy of the protein in d All of the above e None of ※ 1. Cleavage of an IgG molecule by the protease, papain, produces a an antigen -bind ing site and two constant regions B two heavy chain-light chain dimers C an inactive mixture of oligopeptides d two Fab fragments and one Fc fragment E an antibody without its N-linked oligosaccharide 2. Antibodies of the Igg class
3. If Anfinsen had not determined the location of the S-S bonds in renatured RNaseA, his result of >90% recovery of enzyme activity would A have proven his hypothesis. B not have been believed. C not have been possible. D have been hard to believe. E have gone unnoticed. 4. The statement (from Campbell, p.127) that "the amino acid sequence of a protein contains all of the information required for the complete three dimensional structure" A cannot be falsified by experiment; hence it is trivial. B is strongly supported by many denaturation-renaturation experiments. C is called an "hypothesis" since its validity is sort of dicey. D is called a "model" because it can be diagrammed in textbooks. E has essentially been proven by recent theoretical work. 5. Anfinsen probably chose RNaseA for his experiments instead of say, trypsin or chymotrypsin, because A trypsin would digest itself to oligopeptides under mildly denaturing conditions (slow removal of urea). B RNaseA is less expensive than trypsin or chymotrypsin. C Trypsin and chymotrypsin are intracellular enzymes (no S-S bonds). D RNaseA has only 25 amino acid residues. E RNaseA does not have any interfering His residues. 6. Which of the following occurred when RNaseA refolded? A The primary structure of the protein was rearranged. B Most of the charged residues were found buried in the protein. C The entropy of the protein increased. D All of the above. E None of the above. 5 ※ 1. Cleavage of an IgG molecule by the protease, papain, produces: A an antigen-binding site and two constant regions. B two heavy chain-light chain dimers. C an inactive mixture of oligopeptides. D two Fab fragments and one Fc fragment. E an antibody without its N-linked oligosaccharide. 2. Antibodies of the IgG class
a consist of four subunits B are glycoproteins c have inter- and intra-chain d sulfide crosslinks d are secreted into the blood stream E All four choices are correct 3. The immunoglobulin fold a found only in Igg molecules b composed of two antiparallel b-strands folded into a globular domain c a b-barrel composed of a three -and a four-stranded antiparallel b-sheet d found six times in the lgg molecule e The third and fourth choices are both correct 4. Antigenic determinants bind to which portions of an antibody? a variable regions B constant regions c only light chain d only heavy chains e the effector region 5. Monoclonal antibod ies produced in the laboratory a lack the constant regions of IgG b cannot be used for disease diagnosis yet c derive from human cancer patients d can be selected to bind to almost any known molecule e None of the above are correct 6. Antibodies in the human immune system can identify approximately 108 different molecules. Which one of the following is true? a This diversity is generated from 108 different immunoglobin genes b Most of these antibodies recognize self-antigens C Most of these antibodies recognize proteins. D Most of these antibodies recognize small organic molecules e There are really just a small number of antibodies, each of which can bind to many different antiger gon ※<8 1. The specificity of a ligand bind ing site on a protein is based on a the absence of competing ligands b the amino acid residues lining the bind ing site. c the presence of hydrating water molecules
A consist of four subunits. B are glycoproteins. C have inter- and intra-chain disulfide crosslinks. D are secreted into the bloodstream. E All four choices are correct. 3. The immunoglobulin fold is A found only in IgG molecules. B composed of two antiparallel b-strands folded into a globular domain. C a b-barrel composed of a three- and a four-stranded antiparallel b-sheet. D found six times in the IgG molecule. E The third and fourth choices are both correct. 4. Antigenic determinants bind to which portions of an antibody? A variable regions. B constant regions. C only light chains. D only heavy chains. E the effector region. 5. Monoclonal antibodies produced in the laboratory A lack the constant regions of IgG. B cannot be used for disease diagnosis yet. C derive from human cancer patients. D can be selected to bind to almost any known molecule. E None of the above are correct. 6. Antibodies in the human immune system can identify approximately 108 different molecules. Which one of the following is true? A This diversity is generated from 108 different immunoglobin genes. B Most of these antibodies recognize self-antigens. C Most of these antibodies recognize proteins. D Most of these antibodies recognize small organic molecules. E There are really just a small number of antibodies, each of which can bind to many different antigens. F have gone unnoticed. 5 ※ 1. The specificity of a ligand binding site on a protein is based on: A the absence of competing ligands. B the amino acid residues lining the binding site. C the presence of hydrating water molecules
