Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 31, Problem 30P
Interpretation Introduction
Interpretation:
The functions of protein factors in protein synthesis should be determined.
Concept introduction:
Protein synthesis (translation) is a process of generating new protein sequences inside the cell. This process takes place in the cytoplasm of the cell. This process is balanced by the degradation or export of cellular proteins. It is constituted of three steps namely, initiation, elongation, and termination.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Exponential expansion? Compare the amount of information inherent in the genome, the proteome, and the glycome.
Protein folding with PDI and Peptidyl-prolyl isomerase
Etiology? What does that mean? What does the fact that rotenone appears to increase the susceptibility to Parkinson disease indicate about the etiology of Parkinson disease?
Chapter 31 Solutions
Biochemistry
Ch. 31 - Prob. 1PCh. 31 - Prob. 2PCh. 31 - Prob. 3PCh. 31 - Prob. 4PCh. 31 - Prob. 5PCh. 31 - Prob. 6PCh. 31 - Prob. 7PCh. 31 - Prob. 8PCh. 31 - Prob. 9PCh. 31 - Prob. 10P
Ch. 31 - Prob. 11PCh. 31 - Prob. 12PCh. 31 - Prob. 13PCh. 31 - Prob. 14PCh. 31 - Prob. 15PCh. 31 - Prob. 16PCh. 31 - Prob. 17PCh. 31 - Prob. 18PCh. 31 - Prob. 19PCh. 31 - Prob. 20PCh. 31 - Prob. 21PCh. 31 - Prob. 22PCh. 31 - Prob. 23PCh. 31 - Prob. 24PCh. 31 - Prob. 25PCh. 31 - Prob. 26PCh. 31 - Prob. 27PCh. 31 - Prob. 28PCh. 31 - Prob. 29PCh. 31 - Prob. 30PCh. 31 - Prob. 31PCh. 31 - Prob. 32PCh. 31 - Prob. 33PCh. 31 - Prob. 34PCh. 31 - Prob. 35PCh. 31 - Prob. 36PCh. 31 - Prob. 37PCh. 31 - Prob. 38PCh. 31 - Prob. 39PCh. 31 - Prob. 40PCh. 31 - Prob. 41PCh. 31 - Prob. 42PCh. 31 - Prob. 43PCh. 31 - Prob. 44PCh. 31 - Prob. 45PCh. 31 - Prob. 46PCh. 31 - Prob. 47PCh. 31 - Prob. 48PCh. 31 - Prob. 49PCh. 31 - Prob. 50PCh. 31 - Prob. 51PCh. 31 - Prob. 52P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Straight or with a twist? Account for the different structures of glycogen and cellulose.arrow_forwardDisadvantages of cholesterolarrow_forwardActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartatearrow_forward
- Mutation identity- GLY Outline the effects the mutation will have on the 3D structure and function of the 3GRS glucathione reducatse protein.arrow_forwardModified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.arrow_forwardhow many amino acids and omega bonds? How many amino acids appear to have undergone a post-translational modification? how many amino acids which would be classified as polar uncharged amino acids?arrow_forward
- Serine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surelyarrow_forwardBIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : In human beings, what is the major control of de novo pyrimidine nucleotide synthesis? A. substrate availability B. competitive inhibition of carbamoyl phosphate synthetase II C. feedback inhibition of glutamine-PRPP amidotransferase D. vailability of N-acetyl glutamatearrow_forwardActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1 Alanyl-phenylalanine 2. Lysyl-alanine 3.Phenylalanyl-tyrosyl-leucinearrow_forward
- resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?arrow_forwardcip sequence rule in ephedrinearrow_forwardbiosynthesis of Thymidine monophosphate from ATP, HCO3-, Gln, Asp, quinone, and methylene THF. Show your work and don’t forget that the conversion of U to T only happens AFTER Ribonucleotide Reductase processes the 2’, 3’ ribose to the 3’ deoxy ribosearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY