Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 12.4, Problem 2EQ
Summary Introduction
To explain: The benefit of using the radio labeled amino acid in the experiment done by Nirenberg and Leder experiment.
Introduction: The triplet is the RNA molecules containing the set of three nucleotides. The triples had the special characteristics of causing the tRNA molecule to bind to a ribosome. The two scientists, Nirenberg and Leder discovered the concept of triplets in the mRNA molecules.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
firt imagine right side
An SDS-PAGE electrophoresis obtained after protein extraction is shown in Figure 1. Protein kaleidoscope standards and precision were present in Well 1 (far right). Laemmle + DTT was in well number two. Precision plus protein unstained standards, which aid in the identification of protein sizes, were present in Well 3. Catfish protein extract was present in well 4. Cod protein extract from cod was found in well 5. Flounder protein extract was found in well 6. Trout Protein extract from swordfish was found in well 7. Tuna protein extract was present in well 8. Standards for Actin and Myosin were found in Well 9. Lastly, Laemmle was found in well 9. As shown on the left, the protein sizes varied from 10 kD to 250 kD. analyze please ?
second imagine rigth side please
Figure 2 depicts a membrane after western blotting. Well 1, located on the far left, featured precise and protein-rich kaleidoscopic standards that aided in the identification of protein sizes. The…
What was the benefit of using radiolabeled aminoacids in the Nirenberg and Leder experiment?
Does the Hershy-Chase experiment distinguish between DNA and RNA as the molecular
serving as the genetic material? Why or why not?
Chapter 12 Solutions
Biology
Ch. 12.1 - What disease would result if a person inherited...Ch. 12.1 - Prob. 2CCCh. 12.1 - What is the direction of flow of genetic...Ch. 12.2 - Core Skill: Connections Look back at the role of...Ch. 12.3 - Prob. 1CCCh. 12.4 - Prob. 1CCCh. 12.4 - Prob. 1EQCh. 12.4 - Prob. 2EQCh. 12.4 - Prob. 3EQCh. 12.5 - Core Skill: Connections Look back at Figure 6.3,...
Ch. 12.5 - Prob. 2CSCh. 12.6 - Prob. 1CCCh. 12 - Which of the following best represents the central...Ch. 12 - A mutation prevents a gene from being transcribed...Ch. 12 - Prob. 3TYCh. 12 - Prob. 4TYCh. 12 - If a eukaryotic mRNA failed to have a cap attached...Ch. 12 - Prob. 6TYCh. 12 - Prob. 7TYCh. 12 - During the initiation of translation, the first...Ch. 12 - Prob. 9TYCh. 12 - Prob. 10TYCh. 12 - Prob. 1CQCh. 12 - Prob. 2CQCh. 12 - Prob. 3CQCh. 12 - Prob. 1COQCh. 12 - Prob. 2COQ
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- biochem question Write and draw out the three-letter abbreviation of the amino acid sequence histidine,alanine,asparagine,alanine,histidine. Using the pka values calculate the isoelectric point of that amino acid sequence. include c and n terminus for amino acids with no pH. pka c term= 2, pka n term=9, pH of histidine is 6.04. then indicate which two pKa were used to calculate the pl. thank youarrow_forwardbiochem question Write and draw out the three-letter abbreviation of the amino acid sequence histidine,alanine,asparagine,alanine,histidine. Using the pka values calculate the isoelectric point of that amino acid sequence. include c and n terminus for amino acids with no pH. pkac term= 2, pka n term=9, pH of histidine is 6.04. then indicate which two pKa were used to calculate the pl. thank youarrow_forwardQ4 (a) SDS-PAGE. Sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) is used to identify the molecular weight of unknown protein samples. Briefly outline the principle of SDS-PAGE. Marks: 2 For the toolbar, press ALT+F10 (PC) or ALT+FN+F10 (Mac). BIUS E v E Y A ... Paragraph Arial 14pxarrow_forward
- . Brifely describe the difference between Zero oreer, First order and Hugher order NMR Spectra??arrow_forwardBriefly describe the importance of two dimensional electrophoresis in protein separation?arrow_forwardWhich of the following is used extensively in biochemicaland genetic work ?(a) Agaricus (b) Alternaria(c) Neurospora (d) Mucor Please try to break the solutions into as many steps as practically possible and the steps should come one by one and they should be short and crisp and plagiarism-free.arrow_forward
- (b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.arrow_forwardPlease explain!!! select all that are right the same Protein X was purified from tissue source A and tissue source B, yielding the following results: Protein X, sample A: specific activity = 100 U/mg; fold-purification = 200 Protein X, sample B: specific activity = 1000 U/mg; fold-purification = 100 Which of the following statements are correct? a) Protein X, sample A has a higher level of purity than Protein X, sample B. b) Protein X, sample B has a higher level of purity than Protein X, sample A. c) Tissue source A has a higher specific activity for Protein X than tissue source B. d) Tissue source B has a higher specific activity for Protein X than tissue source A.arrow_forwardHow can molecular structural analysis be accomplished with electrospray ionization mass spectrometry?arrow_forward
- What is the biochemical advantage of sigmoidal kinetcs?arrow_forwardWhat is the 1% extinction value of the protein used to calibrate this experiment? I obtained a gradient of 0.0021, into which units should this be presented?arrow_forwardQuestion: Which base (A, C, T or G) corresponds to X in the unknown? I did the experiment, got the data below, and calculated the binding constants. But I am TOTALLY lost as to how to figure this out! I don't even know what steps I would take. Base pairs Data – all had Temp = 250C PH = 7 Binding Constant A & X [A] = 0.00373221M [X] = 0.00373221M [AX] = 0.0462678M 3.322 C & X [C] = 0.0469007M [X] = 0.0469007M [CX] = 0.00309935M 1.409 T & X [T] = 0.0452279M [X] = 0.0452279M [TX] = 0.00477212M 2.333 G & X [G] = 0.0469554M [X] = 0.0469554M [GX] = 0.00304456M 2.633arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Case Studies In Health Information ManagementBiologyISBN:9781337676908Author:SCHNERINGPublisher:Cengage
Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Case Studies In Health Information Management
Biology
ISBN:9781337676908
Author:SCHNERING
Publisher:Cengage
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning
DNA vs RNA (Updated); Author: Amoeba Sisters;https://www.youtube.com/watch?v=JQByjprj_mA;License: Standard youtube license