A Phe Cys «N-terminus Cys Met Cys- C-terminus B

Q: In the image attached, there are 4 nitrogenous bases plus ribose used to generate strands of DNA.…

A: Note: As per the authoring guidelines solving only the first question (A). Repost all others,…

Q: Two peptide segments are shown below. Predict which one would have the most negative AG when going…

A: Protein folding is a spontaneous reaction by which most of the proteins fold inside the cell without…

Q: A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu,…

A: Small molecules called amino acids form the building blocks of proteins. In chemistry, an amino acid…

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: Long-range interactions between residues on a single polypeptide chain are classified as quaternary…

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

Q: The sequence of a 29 aa long peptide can be determined from the following data. a) Treatment of the…

A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…

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: Pompe disease is a rare genetic condition resulting from a deficiency of the protein…

A: Pompe disease is a genetic disorder that involves the accumulation of glycogen inside the cells.…

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: Draw the arrow-pushing mechanism for this knowing that histidine amino acid residue acts as a…

A:

Q: . Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold).…

A: In disulfide linkage, the two cysteine amino acids are joined by a disulfide bond.

Q: Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold).…

A: Disulfide bonds are considered the covalent bond, which is formed between the two cysteine residues.…

Q: A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3…

A: Amino acids are organic compounds that combine to form proteins. Amino acids and proteins are the…

Q: Suppose that there is an unknown protein that underwent Edman sequencing method. From N- terminal…

A: Sequencing of proteins is done by treating Proteins with different enzymes that have specificity in…

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: You are studying the toxic protein called ectatomin, a major component of ant venom (specifically…

A: Proteins contain amino acids. They are linked to each other by peptide bonds. The amino acid such as…

Q: In the amino acid sequence below, the amino acid residue in red was shown to be essential to the…

A: Peptides or proteins are composed of twenty standard amino acids. These standard amino acids differ…

Q: Which of the following is true about formation of the secondary structure features, a-helices or a…

A: Proteins are the ultimate products of the genes. DNA is transcribed into m RNA and this is…

Q: The effect of base-pair substitution mutations on protein function varies widely from no detectable…

A: It is because of the protein functionality isn't affected by the mutations occurred in the intron…

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: An oligopeptide has seven amide linkages (or eight amino acid residues, including the terminal…

A: The alpha helix is a common motif in the secondary structure of proteins and is a right hand-helix…

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: An oligopeptide has nine amide linkages (or ten amino acid residues, include the terminal carboxyl…

A: The primary structure of proteins is composed of amino acid sequences. Alpha helix (helical) and…

Q: The pK1, pK2, and pKR of the amino acid lysine are 2.2, 9.1, and 10.5, respectively. The pK1, pK2,…

A: Proteins can be successfully separated using many different techniques. Chromatography is the…

Q: You have discovered a novel protein that has a pI = 5.5. To study the functional properties of this…

A: Isoelectric Point (pI) is a condition at a particular pH where the amino acid is present in the…

Q: You have discovered a novel protein that has a pI = 5.5. To study the functional properties of this…

A: The functional properties of the new protein, has two amino acid changes—namely, a surface Phe…

Q: why do you think this is? In your explanation, you should describe the specific molecular…

A: 1. Proline is rarely found in beta sheets or alpha helices this is because proline is totally…

Q: . A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3…

A: Chymotrypsin cleaves the peptide bond towards carboxy side of phenylalanine residue. Cyanogen…

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: Given the following sequence, what secondary structure does it most likely prefer, and where in a…

A: The amino acids are the smallest subunit or monomer of the proteins. These amino acids are…

Q: What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9.…

A: The above peptide sequence is made up of five amino acids. First is Lysine, second valine, third…

Q: You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino…

A: In biochemistry, pH can be referred as the decimal logarithmic value of the reciprocal of H+…

Q: Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh?

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

Q: Partial hydrolysis of a protein yielded a number of polypeptides. One of them was purified. Deduce…

A: Complete acid hydrolysis yielded ala + arg + 2ser + lys + phe + met + trp + pro. So we know the…

Q: Draw out this peptide using condensed or line-bond structures: His-Thy-Phe-Cys-Glu examine your…

A: Given sequence,  His-Thy-Phe-Cys-Glu His - Histidine  Thr - Threonine Phe -Phenylalanine Cys -…

Q: It is often the case that a helices are positioned in a protein such that one side faces the…

A: Introduction As the name implies, an amphipathic (or amphiphilic) helix is an α-helix with both…

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: 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: The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in the solvent.…

A: Mass spectroscopy : It is an analytical technique that is used to measure the mass-to-change ratio…

Q: Using the standard 3.6 amino acids per turn (360°) and the helical wheel below, plot each sequence…

A: A helical wheel is a visual representation of amino acids that is used to illustrate the alpha…

Q: Trypsin cleaves a polypeptide backbone at the C-terminal side of Arg or Lys residues, whereas…

A: Polypeptide is formed when amino acids are joined together with peptide bonds. Peptide bond is…

Q: The molecular weight of an unspecified protein, is 70,000 Dalton, as determined by gel filtration…

A: ELlectrophoretic separation of proteins is most commonly performed in polyacrylamide gels. The…

Q: The folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu…

A: The protein property depends on the amino acid property.

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.