[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"detail-sidebar-cat-0-en-105":3,"doc-seo-455840-105":59,"doc-detail-455840-en":131},{"code":4,"msg":5,"data":6},0,"success",[7,13,18,23,28,33,38,43,48,51,55],{"id":8,"doc_module":4,"doc_module_name":9,"category_name":10,"show_sort_weight":11,"slug":12},1,"Document","Story & Novel",90,"story-novel",{"id":14,"doc_module":4,"doc_module_name":9,"category_name":15,"show_sort_weight":16,"slug":17},2,"Literature",80,"literature",{"id":19,"doc_module":4,"doc_module_name":9,"category_name":20,"show_sort_weight":21,"slug":22},4,"Exam",70,"exam",{"id":24,"doc_module":4,"doc_module_name":9,"category_name":25,"show_sort_weight":26,"slug":27},5,"Comic",60,"comic",{"id":29,"doc_module":4,"doc_module_name":9,"category_name":30,"show_sort_weight":31,"slug":32},6,"Technology",50,"technology",{"id":34,"doc_module":4,"doc_module_name":9,"category_name":35,"show_sort_weight":36,"slug":37},7,"Healthcare",40,"healthcare",{"id":39,"doc_module":4,"doc_module_name":9,"category_name":40,"show_sort_weight":41,"slug":42},8,"Research & Report",30,"research-report",{"id":44,"doc_module":4,"doc_module_name":9,"category_name":45,"show_sort_weight":46,"slug":47},9,"Religion & Spirituality",20,"religion-spirituality",{"id":46,"doc_module":4,"doc_module_name":9,"category_name":49,"show_sort_weight":46,"slug":50},"World Cup","world-cup",{"id":52,"doc_module":4,"doc_module_name":9,"category_name":53,"show_sort_weight":52,"slug":54},10,"Lifestyle","lifestyle",{"id":56,"doc_module":4,"doc_module_name":9,"category_name":57,"show_sort_weight":24,"slug":58},19,"General","general",{"code":4,"msg":60,"data":61},"ok",{"site_id":62,"language":63,"slug":64,"title":65,"keywords":66,"description":67,"schema_data":68,"social_meta":124,"head_meta":126,"extra_data":128,"updated_unix":130},105,"en","final-exam-i-245-points","FINAL EXAM I - 245 points","","Biochemistry exam preparation material for a “Final Exam I” assessment, covering key topics in enzyme kinetics, protein structure and folding, amino acid properties, buffer selection using pKa/Ka values, and macromolecular interactions. Multiple-choice questions emphasize interpreting biochemical mechanisms such as Michaelis–Menten behavior, substrate efficiency, peptide-bond geometry, and DNA/protein synthesis fundamentals. The document includes scoring allocation across question sets and a total points summary for the exam sections.",{"@graph":69,"@context":123},[70,84,106],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":20,"@type":76,"position":81},"https://docshare.wps.com/document/exam/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/final-exam-i-245-points/455840/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/final-exam-i-245-points/455840.png","ImageObject",300,407,{"name":92,"@type":93},"moss~","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-26","2026-09-30",true,{"@type":102,"interactionType":103,"userInteractionCount":105},"InteractionCounter",{"@type":104},"ViewAction",24,{"@type":107,"mainEntity":108},"FAQPage",[109,115,119],{"name":110,"@type":111,"acceptedAnswer":112},"How are points distributed across the multiple-choice questions?","Question",{"text":113,"@type":114},"Questions 1–17 are worth 10 points each (170 points total), and questions 18–32 are worth 5 points each (75 points total), for a total of 245 points in this part.","Answer",{"name":116,"@type":111,"acceptedAnswer":117},"What does the pH-related buffer question require you to select?",{"text":118,"@type":114},"It asks which acid and conjugate base pair, using the listed Ka values, is best for maintaining pH 4.0 for an enzyme reaction.",{"name":120,"@type":111,"acceptedAnswer":121},"According to the enzyme-kinetics question, which Michaelis–Menten statement is false?",{"text":122,"@type":114},"The exam provides five statements about Michaelis–Menten kinetics (Km definition, inhibitor effects, saturation behavior, time dependence of rate, and activation/equilibrium relationships) and asks you to choose the false one.","https://schema.org",{"og:url":83,"og:type":125,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":127,"canonical":83},"index,follow",{"doc_id":129,"site_id":62},455840,1790820682,{"code":4,"msg":5,"data":132},{"doc_id":129,"user_id":133,"nickname":92,"user_avatar":134,"doc_module":4,"category_id":19,"category_name":20,"doc_title":65,"doc_description":67,"doc_content":135,"file_id":136,"file_url":137,"file_type":138,"file_size":139,"view_count":105,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":140,"language":141,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":142,"faqs":143,"seo_title":144,"seo_description":67,"update_tm":145,"read_time":41},962090895452,"https://ap-avatar.wpscdn.com/davatar_a8503ba1806abce46bf441b54a3ca4cd","NAME    \nFINAL EXAM I .   /245  \nDecember 19, 1998  \nBiochemistry I II .__________________ / 50  \nBI/CH421, BI601, BI/CH621  \nIII .__________________ / 32  \nIV .__________________ / 73  \nTOTAL /400  \nI . MULTIPLE CHOICE  (245 points)  \nChoose the BEST answer to the question by circling the appropriate letter . Questions 1-17 are worth 10 points each (170 pts . ) and questions 18-32 are worth 5 points each (75 pts . ) .  \n1. An enzyme reaction to be studied at pH 4.0 can best be carried out using a buffer solution made from which of the following acids, and their conjugate bases, with Ka values as shown? (Assume that there is no direct interaction between the buffer molecule and the enzyme to be studied. )  \n Acid Ka   \nA . Phosphoric acid 7.3 x 10-3  \nB . Lactic acid 1.4 x 10-4  \nC . Acetic acid 1.2 x 10-5  \nD . Dihydrogen phosphate ion (H2 PO 4- ) 6.3 x 10-8  \nE . Bicarbonate ion (HCO 3- ) 6.3 x 10-11  \n2. In the diagram below, the plane drawn behind the peptide bond indicates the:  \nA . plane of rotation around the Ca-N bond .  \nB . absence of rotation around the C-N bond because of its partial double bond character .  \nC . region of steric hindrance determined by the large C=O group .  \nD . theoretical space between-180􀂰 and +180􀂰 that can be occupied by the j and f angles in the peptide bond .  \nE . region of the peptide bond that contributes to a Ramachandran plot .  \nNAME    \n3. Which of the following amino acids is the most soluble in water at pH 7 .0?  \nA . Glutamate  \nB . Tryptophan  \nC . Leucine  \nD . Tyrosine  \nE . Phenylalanine  \n4. The folded states of globular proteins in aqueous solutions are stabilized primarily by   .  \nA . hydrophobic interactions  \nB . peptide bonds  \nC . phosphodiester bonds  \nD . ionic bonds  \nE . disulfide bonds  \n5. Which of these statements about enzyme-catalyzed reactions that obey Michaelis-Menten kinetics is false?  \nA . At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration.  \nB . The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax .  \nC . If enough substrate is added, the normal Vmax of a reaction can be attained even in the presence of a competitive inhibitor.  \nD . The rate of a reaction decreases steadily with time as substrate is depleted .  \nE . The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction.  \n6. The most efficient substrate of an enzyme is usually considered to bethe substrate with the   .  \nA . largest k cat  \nB . largest Km  \nC . largest k cat/Km  \nD . smallest k cat/Km  \nE . smallest Km  \n7. Certain restriction enzymes produce cohesive (sticky) ends . This means that they:  \nA . cut in regions of high GC content, leaving ends that can form more hydrogen bonds than ends of high AT content .  \nB . make a staggered double-strand cut, leaving ends with a few nucleotides of single-stranded DNA protruding.  \nC . cut both DNA strands at the same base pair.  \nD . stick tightly to the ends of the DNA it has cut .  \nE . have none of the above characteristics.  \nNAME    \n8. Two oligo-deoxynucleotides, 5' -ACCACGTAACGGA-3' and 5' -GTTAC-3', plus DNA polymerase are added to a reaction mixture containing the appropriate buffer plus radiolabelled dATP, dTTP, dCTP, and dGTP . The radiolabelled bases incorporated into the product of such a reaction would have which of the following base compositions?  \nA . 3C:2A  \nB . 1G:1T  \nC . 3G:2T  \nD . 3G:3T:2C  \nE . 5T:4G:3C:1A  \n9. A = 27% G = 30% T = 21% C = 22%  \nIf the genome of a newly isolated virus displays the base composition above, the virus most likely consists of   .  \nA . single-stranded DNA  \nB . double-stranded DNA  \nC . single-stranded RNA  \nD . double-stranded RNA  \nE . a double-stranded RNA:DNA heteroduplex  \n10. For protein synthesis, an amino acid needs to be attached by its   group to the   of the tRNA molecule .  \nA . am","cbCaitcJEwIZF1N7","https://ap.wps.com/l/cbCaitcJEwIZF1N7","pdf",613177,12,"English","# MULTIPLE CHOICE\n## Enzyme kinetics and buffering\n## Protein structure, amino acids, and folding\n## Nucleic acids, translation, and inhibitors\n## Protein precipitation and pH questions","[{\"question\":\"How are points distributed across the multiple-choice questions?\",\"answer\":\"Questions 1–17 are worth 10 points each (170 points total), and questions 18–32 are worth 5 points each (75 points total), for a total of 245 points in this part.\"},{\"question\":\"What does the pH-related buffer question require you to select?\",\"answer\":\"It asks which acid and conjugate base pair, using the listed Ka values, is best for maintaining pH 4.0 for an enzyme reaction.\"},{\"question\":\"According to the enzyme-kinetics question, which Michaelis–Menten statement is false?\",\"answer\":\"The exam provides five statements about Michaelis–Menten kinetics (Km definition, inhibitor effects, saturation behavior, time dependence of rate, and activation/equilibrium relationships) and asks you to choose the false one.\"}]","FINAL EXAM I - 245 points | PDF",1790744455]