Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 31, Problem 2P
Interpretation Introduction
Interpretation:
The fact regarding the structural consequences of proteolytic nicks in proteins needs to be explained.
Concept Introduction:
Ub or Ubiquitin is the 76-residue protein which is present within the cells. They areeither free or conjugated covalently towards each other. Ubiquitin is present in all the eukaryotes, but seemingly not present in prokaryotes. Amid eukaryotes, Ubiquitin is considered as the mostconserved proteins.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Full length resilin that is not in a cell is thought by some to form a tertiary structure of this form (picture attached)
The yellow portions represent exon 1 and the blue portions exon 3. These structures assemble into a kind of lattice or network. In full length resilin, stress in the form of mechanical pressure or heating to remove water results in a tighter network that excludes any water internally.
How might this behavior of resilin produce its ‘elasticity’? Explain how the looser water containing structure and the tighter water excluding structure may give us a mechanism for the elasticity.
Please correct answer and don't use hend raiting
Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent?
Your reply will be greatly appreciated.
The ligand that was assigned to me is tadalafil.
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
- Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.arrow_forwardThe Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?arrow_forwardUnderstanding the Nature of the Ubiquitin-Ubiquitin linkage Draw the structure of the isopeptide bond formed between Gly76of one ubiquitin molecule and Lys48of another ubiquitin molecule.arrow_forward
- Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.arrow_forwardHi - I have the following as a question in my biochemistry course and I am just lost on where to start. Thanks! Cyt cb562 will form a tetramer in the presence of Zn+2 or in the absence of Zn+2, it will form a trimer. For both the tetramer and the trimer, suggest the identity of three different amino acids that could be on the interface. Explain how your selections facilitate these interactions.arrow_forwardHydropathy & Amphipathicity 2 -1 -2- 110 210 310 410 510 Residue Number C. Draw the topology of this membrane protein in the bilayer and indicate the range of residues forming transmembrane a-helices.arrow_forward
- .A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little if any effect from addingarrow_forwardcip sequence rule in ephedrinearrow_forwardWhat is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue protein, starting from amino acids? Assume that the hydrolysis of PP i is equivalent to the hydrolysis of ATP for this calculation.arrow_forward
- Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.arrow_forwardThe allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!arrow_forwardplease provide answer to these question i failed itarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning
Biology: The Unity and Diversity of Life (MindTap...BiologyISBN:9781305073951Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa StarrPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...
Biology
ISBN:9781305251052
Author:Michael Cummings
Publisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)
Biology
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Cengage Learning
Biology: The Unity and Diversity of Life (MindTap...
Biology
ISBN:9781305073951
Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr
Publisher:Cengage Learning
QCE Biology: Introduction to Gene Expression; Author: Atomi;https://www.youtube.com/watch?v=a7hydUtCIJk;License: Standard YouTube License, CC-BY