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 14, Problem 2P
Interpretation Introduction
Interpretation:
Whether SH2 domains bind phosphoserine and phosphothreonine with high affinity or not needs to be explained.
Concept introduction:
SH2 is a type of structurally conserved protein which is contained within the Src onco protein and is also present in the signal transducing protein. It is a protein domain of around 100 protein residues.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Amino acids at the interaction site ( F,I and L) and its G protein partner (P, L, Y) are very conserved.If the amino acids are swapped between the protein and GPCR is binding expected to be as tight?
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine?
In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
high and low affinity binding sites require the same amount of ligand to achieve saturation
true or false?
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
- Consider a globular protein that contains an alpha-helix within it: a) Suppose there is a ligand binding pocket in this alpha-helix that contains residues of Leu (2), Phe (5), Gly (6), Ala (18), Tyr (22), Tyr (28), Gly (30), Cys (45), His (48) and Asp (49). What does this tell us about the likely nature or characteristics of a potential binding ligand? I said tha because 6/10 of the amino acids in this binding pocket are non-polar, that the ligand is also non-polar, but I think the question needs more description about the ligand. b) Briefly describe the driving forces and energetics behind folding of globular proteins (use terms like ΔH, ΔS, and ΔG) I said that H = -, S = +, G = - Folding driving force would likely be entropy change from non-polar residues interacting with a solvent (ex: water). Hence, non-polar residues would be buried in the globular protein structure from folding, causing entropy to increase for any liberated solvent molecules. Not 100% sure if this is correct,…arrow_forwardWhy does CTP favor the T state while ATP favors the R state? (in reference to CTPase).arrow_forwardEven though the actual concentration inside a cell is above critical concentration, 50% of action is in monomeric form. Explain how the cell maintains monomeric actin above critical concentration ?arrow_forward
- A family of proteins known as cupredoxins contain a single redoxactive Cu ion coordinated by a Cys, a Met, and two His residues. The reduction potentials of cupredoxins range from about 0.15 V to 0.68 V. What does this information reveal about the role of the protein component of the cupredoxins?arrow_forwardIn the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.arrow_forwardSome hormone-signaling pathways result in the phosphorylation of tyrosine resides in proteins. Draw the structure of a phosphotyrosine side chain.arrow_forward
- a) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?arrow_forward12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.arrow_forwardExplain why a protein tyrosine phosphatase would include an SH2 domain in addition to its phosphatase domain.arrow_forward
- Disulfide linkages are uncommon in cytoplasmic proteins, whereas they are common in extracellular proteins. Why?arrow_forwardConsider the binding reaction L + R → LR, where L is a ligand and R is its receptor. When 1 × 10−3 M of L is added to a solution containing 5 × 10−2 M of R, 90 percent of the L binds to form LR. What is the Keq of this reaction? How will the Keq be affected by the addition of a protein that facilitates (catalyzes) this binding reaction? What is the dissociation equilibrium constant Kd?arrow_forwardChymotrypsin preferentially binds the transition state. What is meant by that?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningHuman Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher: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
Metabolic Pathways; Author: Wisc-Online;https://www.youtube.com/watch?v=m61bQYio9ys;License: Standard Youtube License