Which of the following statements are correct about the role of chaperones in protein folding (select all that appy)?   A. Chaperones accelerate the rate of protein folding   B. Presence of chaperones contradicts dogma that structure of protein is only determined by amino acid sequence   C. Chapreone promotion of native folding is an ATP-dependent process   D. Chaperones work by stabilizing hydrophobic patches on proteins   E. A cell line with the GroEL and GroES deleted would accumulate more unfolded protein

Q: Protein A binds ligand B. You incubate protein A in a solution of ligand B. The concentration of…

A: The fractional occupancy is the term often used in ligand and receptor interaction. This term is…

Q: A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U).…

A: The formation of a ligand-protein complex is an exothermic process with a ΔH equal to the binding…

Q: Electrostatic interactions are the dominant forces in protein molecular recognition.

A: Since you have asked multiple question, we will solve the first question for you. If you want any…

Q: Consider five proteins with the properties shown in the following table. Answer the questions below…

A: Protein is an organic nitrogenous macromolecule that is essential for the health of humans. In the…

Q: Which of the following statements are correct about protein folding (select all that appy)?   A.…

A: Protein folding is the physical process by which a protein folds into its functional…

Q: a). What is the percentage alpha helical content of the protein? Show your working. b.) The protein…

A: Circular dichroism is a spectroscopic technique to find out the secondary structure, folding and…

Q: The major difference between a protein molecule in its native state and in its denatured state lies…

A: The Native state of a protein is the functional three-dimensional form of a protein. The Native…

Q: Consider a protein in which a negatively charged glutamic acid side chain(pKa = 4.2) makes a salt…

A: Amino acids are organic compounds that contain amine and carboxyl functional groups, along with a…

Q: Proper folding of proteins is essential for their biological activity. In general, the functional…

A: The cells are the primary unit of life. Based on the number of cells an organism may be unicellular…

Q: You are studying a catalytic protein which contains two ion clusters, one cluster contains 2 Cu+3…

A: Proteins are the biomolecules that are building blocks of the body. Proteins are made up of amino…

Q: The amino acid tyrosine contains a phenolic R-group and has pKa values of 2.2, 9.0, and 10.2. A…

A: tyrosine or L-tyrosine is one of the 20 standard amino acids that are used by cells to synthesize…

Q: In cooperative proteins, there is an energetic cost to bind the first molecule. How does this…

A: Cooperative proteins, like hemoglobin, are proteins that are made up of more than one subunit. Each…

Q: A prosthetic group of a protein is a non-protein structure that is: a. a ligand of the protein. b.…

A: Proteins are composed of amino acids. They are linked together by peptide linkages. Proteins have…

Q: The process of a protein folding from an inactive unfolded structure to theactive folded structure…

A: The Native state of a protein is the functional three-dimensional form of a protein. The Native…

Q: a. Suppose that the R group of a histidine residue in a protein in its native tertiary structure is…

A: In the protein, the nonpolar amino acids are usually present in the inner hydrophobic region. Also…

Q: Some point mutations cause a change in amino acid sequence but nonetheless may have little to no…

A: option f is correct . This is  because each group of amino acid belong to same category means . If…

Q: The following data describe binding of ligand A to a protein, using both Scatchard plots and Hills…

A: Scatchard plots is used to determine the affinity of the receptor or any protein for its ligand and…

Q: Suppose there is a ligand binding pocket in this alpha-helix that contains residues of Leu (2), Phe…

A: Globular protein contains van der waals interactions , disulphide bridges , diploar interactions(…

Q: (a) As the pH changes from 9.0 to 5.0, how does the concentration of H+ (protons) change?…

A: pH is a scale used to specify the acidity or basicity of an aqueous solution. Acidic solutions are…

Q: Consider a protein in which a negatively charged glutamic acid side chain (pKa = 4.2) makes a salt…

A: Amino acid is organic compound which contains a carboxyl group, an amino group, and a variable side…

Q: Which statements are true? Protein-protein interfaces are most often dry. The exclusion of water…

A: For an interaction or a reaction to take place spontaneously, or in other words,  for an interaction…

Q: The major difference between a protein molecule in its native state and inits denatured state lies…

A: a. For protein of 100 residues, if in the unfolded state, each bond between the residues has three…

Q: The rate of migration of a protein through an SDS-poly-acrylamide gel is NOT influenced by   A.…

A: The polyacrylamide gel SDS is a kind of analytical technique used to seperate proteins. SDS page is…

Q: When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different…

A: Anfinsen showed that the protein folding data resides within the amino acid sequence of the protein.…

Q: Mutations in proteins do not always lead to a drastic effect on a protein's function. Substitutions…

A: There are 20 amino acids and all are coded by the triplet codons but the overall proteins structure…

Q: Consider the synthesis of a polypeptide by a ribosome of a prokaryote cell. As the polymerization of…

A: The structure of a protein is described as a chain of amino acids linked together by peptide bonds.

Q: Consider the image of the attached protein.  Now imagine you have a proteolytic enzyme that cleaves…

A: The mentioned proteolytic enzyme cleaves the peptide-bonds on the C-terminal sides of basic amino…

Q: Proper folding of proteins is essential for their biological activity. In general, the functional…

A: Chaperons are involved in protein folding.

Q: Theoretical and experimental measurements show that in many cases, thecontributions of ionic and…

A: The folding of proteins is a highly complex mechanism by which proteins are organized into their…

Q: Look at the schematic illustration of a protein (3D conformation) belpw. If the highlighted SER…

A: Proteins are the biomolecules that are made up of Aminoacids joined by Peptide bond. Proteins exist…

Q: Chemistry A biomolecule has a K_d of 1.6mM. A mutated-version of the same biomoleucel was bound by…

A: [P] + [L]   →    [PL] Dissociation constant, Kd = [P] [L] / [PL] Dissociation constant (Kd) - is…

Q: missense mutation will influence the tertiary or quaternary structure of the protein (FGFR3). How…

A: Missense mutation A missense mutation specifically defines the kind of point mutation in which the…

Q: The figure given below shows four possible "folding funnels" for protein folding. Each figure…

A: The folding funnel is a specific version of the energy landscape theory of protein folding, which…

Q: Which of the following statements best describe(s) the mechanism by which correct protein folding…

A: Chaperonin GroEL/GroES is a molecular chaperone that facilitates folding of nascent or denatured…

Q: Do you expect a Pro → Gly mutation in a surface-loop region of a globular protein to be stabilizing…

A: A quantitative measure of the favorability of a given reaction at constant temperature and pressue…

Q: What is one reason that protein folding intermediates are prone to aggregation?   a. Their…

A: Proteins are the macromolecules composed of amino acids bound together by peptide bond between amino…

Q: What is a hydropathy plot, and why is it used? A.A hydropathy plot, is a graph showing the…

A: The hydropathy index is used to find out a minimum stretch of hydrophobic amino acids that can cross…

Q: Which of the following statements are correct about the thermodynamics of protein folding (select…

A: Protein folding can be defined as a process where a chain of protein is translated into its native…

Q: Discuss the role of molecular chaperones in protein folding, and list some important examples of…

A: In molecular biology, the proteins are responsible for assisting in the conformational folding or…

Q: In most cases, mutations in the core of a protein that replace a smaller nonpolar side chain in the…

A: Cells have aqueous environment that is hydrophilic. So, proteins fold in a way that the hydrophilic…

Q: Theoretical and experimental data show that in many cases the ionic and hydrogen-bonding…

A: Proteins are made up of monomeric units of amino acids (primary structure). The polypeptide chains…

Q: Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown…

A: Options 3 and 4 are correct. Acetylation changes tertiary structure of protein and partner protein…

Q: Anfinsen studied protein folding using RNaseA.

A: Proteins are highly sensitive to temperature, pH reducing and denaturing agents.

Q: A protein is made up for two polypeptides that differ in shape.  Each polypeptide has one domain.…

A: The proteins have different levels of structure starting from primary to quaternary structure. The…

Q: Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino…

A: Proteins or peptides have significant roles in our bodies. They are the building blocks of the body.…

Q: Shown is the electrophoretic profile of a pure protein ran at different pH values "H H H H (+) (-)…

A: The net charge of a protein depends on the pH of its environment and the net charge determines the…

Q: pu've isolated a novel protein, but you believe what you actually have is mixture of the unmodified…

A: All the techniques described above in the options use one or more criteria to separate the protein…

Osmosis

In simple words, osmosis is the slow, gradual movement of a liquid through a membrane. But there are nuances to this process. For instance, there has to be an imbalance in the distribution of solute in the liquid on either side of the membrane, which has to be semipermeable. The liquid in the region with a lower solute concentration moves to the region with a higher concentration, thereby displacing the solution in the process. The objective is to equalize the concentration of molecules on both sides of the membrane; the displacement of liquid can be viewed as a byproduct of this equalization. Since there is no energy required to carry osmosis, it is considered a passive process.