Amino acid analysis of a decapeptide gave the following residues:Ala (2), Gly, Leu, Lys (2), Met, Phe, Trp, ValSubjecting the decapeptide to various chemical/ enzymatic hydrolysis yields the following fragments:Cyanogen bromide: Leu-Ala-Met and a heptapeptideTrypsin: Phe-Ala-Lys and a heptapeptideChymotrypsin: Gly-Val-Lys-Phe, Ala-Lys, Leu, and a tripeptide• Thermolysin: Phe-Ala-Lys, Leu-Ala-Met, and two dipeptides.Note that the intact decapeptide was used in each treatment.1. What is the sequence of the heptapeptide produced upon treatment with trypsin? Fill each blank with the three-letter designation of the amino acid residuefrom the N-terminus to the C-terminus.2. What is the sequence of the tripeptide produced upon treatment with chymotrypsin? Fill each blank with the three-letter designation of the amino acidresidues from the N-terminus to the C-terminus.

Specific enzymes have specific cleavage point in amino acids. Chymotrypsin is serine…

Answered: 1. What is the sequence of the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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2. RNA is almost never found in its primary structure and will form secondary structures based on the cellular environment in which it is found. i) Describe why RNA preferentially forms secondary structures and also discuss the major chemical interactions that are facilitating that structure. ii) Below is a structure of an RNA that is folded. This RNA structure can be easily interrupted by addition of Mg2+ to the system. Describe why the secondary RNA structure would change as a result of the addition of this ion. knot 20A 250 S2G 29 G 3" 13 U 10 5' C5 GS1
9. What is the purpose of the following? a) spliceosomes b) RNA polymerase c) Protein release factors d) aminoacyl-tRNA synthetases
#17 #18 please I will give you ?
a. Identify the type of mutation shown below. b. How many amino acids are affected? c. What type of impact will this mutation have on the functionality of the protein? Second Letter UUU UUC UUA JUG UCu uCC UCA UCG UAU UAC UGU UOC Phe Tyr Cys Ser UAA Stop UGA Stop UAG Stop UGG Trp Leu cu cc Pro CUU COU CAU His CAC CUC CUA Leu Arg CCA Cca CGA CUG CAA Cin CAG AGU AGC AGA Arg AAU AUU AUC le AUA AUG Met ACO ACU ACC ACA Asn Ser AAC The MA AAG Lys AGG CAL KAC GUU Aep GUC Val CUA OCC Ala OCA GA Clu GAG Oly GOA GUG GGG Original DNA strand G AC 1. G. G. Mutated DNA strand GA Third letter
1. By use of a labeled diagram or a written description, distinguish the roles of thefollowing in elongation of a polypeptide: initiation complex, charged tRNAs, peptidyltransferase, Site A, Site P 2. What determines the initiation of translation? (Hint: there is more than one feature oftranslation.)
13
1e) Give the sequence of every codon this tRNA, with the anticodon 5'AGG3', could base pair with (perfect and wobble matches), and name the amino acid coded for by each codon whose sequence you have written.
UCUGAUGGGCUUU... Beginning with the Start codon (for Met), which amino acids, in order, are coded for by this section of mRNA? Second letter threonine, methionine, glycine methionine, glycine, phenylalanine methionine, valine, glycine, phenylalanine serine, aspartic acid, glycine, leucine First letter G U UUU phe UUC. UUA UUG CUU CUC CUA CUG Leu Leu GUU GUC GUA GUG AUU AUC lle ACU ACC AUA ACA AUG Met ACG UCU UCC UCA UCG Val CCU CCC CCA CCG GCU GCC GCA GCG Ser Pro Thr Ala CAU CACJ CAA CAG UAU UGU UGC Tyr Cys UAC UAA Stop UGA Stop A UAG Stop UGG Trp G His Gln AAU Asn AAC AAA AAG Lys GAUT GAC GAAT GAG G CGU CGC CGA CGG AGU 1 Ser AGC AGA AGG GGU Asp GGC GGA Glu GGG Arg Arg DUAG DUAU DUAG ULAG Third letter Gly
Which statement is true for the active site residues of RNase A, lysozyme, or trypsin? Select any/all answers that apply. O A. His12 (RNase A) initially acts as an acid. O B. His119 (RNase A) initially acts as an acid. O C. Glu35 (lysozyme) initially acts as an acid. O D. His57 (trypsin) initially acts as an acid. O E. Ser195 (trypsin) initially acts as an acid.
4. A peptide was cleaved into smaller fragments using chymotrypsin and CnBr. The fragments were separated by HPLC and then sequenced by Edman degradation. Determine the sequence of the original peptide from the following fragment sequences. Cleavage with chymotrypsin Cleavage with CnBr EAGPDGMECAF ЕCAFHR GPF CKWEAGPDGM EAAMCKW IAHTYGPFEAAM HR ТАНТY -align the peptides Reagent (source) Trypsin (bovine pancrease) Chymotrypsin (bovine pancrease) Staphylococcus V8 protease Pepsin (porcine pancrease) Cyanogen bromide (chemical)(CnBr) Specificity Lys, Arg (C) Phe, Trp, Tyr (C) Glu, Asp (C) Phe, Trp, Tyr (N) Met (C)
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Give the complementary codons, anticodons, and amino acids for the following: - ATG - CCA-AGG-GCT - ACT Code: TAC-TCG-CGC-ACC-GTA-TGC Give the complementary code, anticodons, and amino acids for the following: Codon: AUG - UCA - UCU - CGU - UAC - CCU - GCC-ACU-GCA - CUG - UAG Give the complementary code, codons, and amino acids for the following: Anticodon : UAC – CUA – GAC – AUG – GGG – CAU – UGG – CCA – GCA – AUU Complete the following tables: CODE: T-A-C A-T-G C-C-G T-G-G A-A-T C-G-C A-T-T CODON: ANTICODON: AMINO ACID: CODE: CODON: ANTICODON: U-A-C A-U-G U-U-C C-G-A AMINO ACID: CODE: CODON: A-U-G ANTICODON AMINO ACID: T-T-A C-C-U A-U-C A-U-C C-C-U A-C-U C-U-G T-A-C U-A-G

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