Consider the phenolic hydroxyl group of a particular Tyr residue in a protein. Suppose the hydroxyl group in the unfolded protein in aqueous solution, where the group is exposed to H2O, has a pKa of 10.0. If that group is found in a hydrophobic environment in the interior of the protein when the protein is folded into its native tertiary structure, would you expect the pKa of the phenolic hydroxyl to be higher or lower in the folded protein interior than in H2O? Explain your reasoning.

Q: Based on the figure and the explanation in the textbook, what are the random chances that the…

A: Denaturation is the process by which proteins lose their native conformation. Ribonuclease A has 124…

Q: Both hsp60-like and hsp70 molecular chaperonesshare an affinity for exposed hydrophobic patches on…

A: Molecular chaperones are defined as the proteins that aid or help in the folding or unfolding of…

Q: The 3° structure of a protein refers to the protein's overall, 3-dimensional shape in space. This…

A: Amino acids are biomolecules that have an amino group, a carboxyl group and a side group that is…

Q: Draw the structure of following peptide: Glu-Asp-His-Cys-Gly-Arg (B) At pH= 10.7 (A) At pH= 2.1

A: Amino acids are organic compounds having two functional group namely carboxyl and amino. Amino acids…

Q: Both hsp60-like and hsp 70 molecular chaperones share an affinity for exposed hydrophobic patches on…

A: Answer: Molecular chaperones are defined as the proteins that aid or help in the folding or…

Q: At physiological pH (i.e. 7.4), polylysine assumes a random structure in solution. Given that the…

A: Protein are complex structures made up of polypeptide chains comprising different amino acids.…

Q: Carboxypeptidase, which sequentially removes carboxyl-terminal amino acid residues from its peptide…

A: Enzymes are a group of proteins that acts as biological catalysts to accelerate the various chemical…

Q: Choose ALL of the charged (+1 or -1) amino acids at aqueous physiological conditions where the ph=…

A: Amino acid is the basic structural unit of proteins. They contain an amino group, a carboxyl group,…

Q: The pKa of the side chain imidazole group of histidine is 6.0. what is the ratio of uncharged to…

A: Amino acids are the monomeric units of proteins. There are 20 amino acids occurring in nature. Amino…

Q: Hydrolysis of dodecapeptide P with the enzyme trypsin affords the following fragments: Glu-Ala-Lys,…

A: Trypsin cleaves the dodecapeptide at the carboxyl side of Lys or Arg. Chymotrypsin cleaves the…

Q: The pi-helix is a rare secondary structural element in proteins that resembles an alpha helix but…

A: Helices are the main secondary structural elements (SSEs) present in protein structures and are…

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: To better understand the effects of palmitoylation on protein X, researchers want to chemically…

A: Palmitoylation is an attachment which is covalent of Palmitic acid, which is a fatty acid to…

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: Saccharide M, a sugar made of repeating units of maltose and cellobiose, is a component of…

A: Glycoproteins are consisted of protein and glycan moiety which is involved in several biological…

Q: Ala-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the…

A: The amino acid molecule possesses the amine (-NH2) and a carboxylic acid (-COOH) functional group…

Q: Let's consider a protein with two surface-exposed histidine residues: • Hisa is a "typical"…

A: The Henderson-Hasselbalch Equation for the deprotonation of a species is given below. pH = pKa +…

Q: In some proteins, the side chain of serine appears to undergo ionization. Explain why ionization…

A: Serine proteases like chymotrypsin are most studied biological enzyme and uses covalent modification…

Q: Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet…

A: Amongst secondary structures of polypeptide chains made of amino acids, β-sheets are a more spacious…

Q: Which amino acid replacement would result in the biggest structural change in a protein if a Cys…

A: Amino Acids Introduction Proteins are polymers made up of nitrogenous chemicals known as amino…

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: In N-linked glycoproteins, the sugar is usually attached to the protein by a bond to the N atom in a…

A: Amino acids are the monomers of the proteins.

Q: Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following…

A: Amino acids are the building blocks of proteins. The amino acid polymer which joins together with…

Q: Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R,…

A: Protein folding is the physical process by which a polypeptide chain is folded into its…

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: Eukaryotic protein X has one proline residue and two cysteine residues. The proline needs to be in…

A: Eukaryotic protein : It is usually the cytoplasmic ribosomes that translate nuclear genes. several…

Q: A sample of the amino acid tyrosine is barely soluble in water. Would a polypeptide containing only…

A: Tyrosine is one of the 20 standard amino acids that are used by calls to synthesize proteins. It is…

Q: You want to treat 10 mL of HL-60 cells with cycloheximide in order to determine the half-life of a…

A: According to Normality Equation,

Q: Imagine a globular protein with a histidine that is involved in a salt bridge to an aspartic acid,…

A: Globular proteins are a group of protein sub-types. They form colloids  and are somewhat soluble in…

Q: The oligopeptide isolated from the brain of an animal has the sequence…

A: Proteins are polypeptide chains formed of monomeric units, amino acids, joined together by a peptide…

Q: Certain polypeptide sequences that show a pronounced tendency to dimerize in an antiparallel…

A: Polypeptides are folded into various secondary protein motifs such as alpha-helix, beta-sheets,…

Q: Assume that some protein molecule, in its folded native state, has one favored conformation. But…

A: "Protein Folding" primarily concerns the comprehensive physical process of transformation from…

Q: Consider a short peptide that forms an alpha-helix within a larger protein structure. Suppose that…

A: Amino acids are the simplest units to form peptides and proteins. The amino acid sequences represent…

Q: Draw the structure of the following peptide as it would be at pH = 7. Does the molecule have a net…

A: The given peptide is composed of methionine, serine, glutamic acid, alanine, two lysine, and…

Q: The β-sheet structure is the secondary structure of the protein which is a sideways folded structure…

A: Protein is an organic nitrogenous macromolecule that is required for human health. In the human…

Q: In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These…

A: Mixed heteropolymer experiment is a test of homology using subunits derived from different species…

Q: list the amino acids that will carry a net charge at pH 7 within a protein. What is the charge at pH…

A: Note : Hi ! Thank you for the question. We are authorized to answer one question at a time. Since…

Q: Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following…

A: An amino acid is a natural atom that is comprised of a fundamental amino gathering (−NH2), an acidic…

Q: A B Amino Acid Lysine Abbreviation 3- Letters Lys 1- Letter K pk₁ -COOH 2.18 pK₂ -NHS* 8.95 PKR R…

A: Amino acids are biomolecules where an alpha carbon is bonded to an amine group , a carboxylic group,…

Q: What does this statement mean: "Upon folding of a protein many main chain amides replace their…

A: Proteins are generally present in an unfolded state after translation, the folding of some proteins…

Q: Consider two proteins, Protein A and Protein B: A is a monomeric protein, whereas B is a subunit of…

A: Proteins are usually made from basic amino acid structures. Thus amino acids are the building blocks…

Q: Explain why the indole nitrogen of tryptophan is more weakly basic than one of the  imidazole…

A: "Since there is multiple question present, I have answered the first question for you. If you need a…

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

A: Mutation : It is an alteration in the nucleotide sequence of the genome of an organism, virus, or…

Q: For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their…

A: Peptides are small chains of amino acids (2-200 residues). pI is the pH at which peptide or…

Q: Suppose that there is a protein consisting of two polypeptide chains with the given sequences in the…

A: Proteins are the polymers of amino acids, joined together by peptide bonds. The amino acid with the…

Q: Lys and Arg Glu and Lys Pro and Asp Among these amino acid combinations listed above, only the…

A: Proteins are composed of a linear chain of amino acids attached together via peptide bonds. All…

Q: Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl…

A: Tyrosine is an essential amino acid. It is a hydroxyl containing aromatic amino acid. It has three…

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.