19.40 Indicate whether each of the following statements describes the primary, secondary, tertiary, or quaternary protein structure: a. Hydrophobic amino acid residues seeking a nonpolar envi- ronment move toward the inside of the folded protein. b. Hydrophilic amino acid residues move to the polar aqueous environment outside the protein. c. An active protein contains four tertiary subunits. d. In sickle cell anemia, valine replaces glutamate in the B-chain.

Q: Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid…

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

Q: From this structure, what is the predominant secondary structure of the protein? Based on what you…

A: Lindsay-Lang proposed the first protein structural hierarchy with four levels: Central, secondary,…

Q: What is the Three-Dimensional Structure of a Protein’s Amino Acid Sequence Dictates?

A: The amino acids join together by peptide bonds. Proteins act as major substrates and reactants for…

Q: When a protein is denatured, how is its primary, secondary, tertiary, and quaternary structure…

A: Proteins are larger macromolecules which are the polymers of amino acids. they are a total of 20…

Q: In what type of intra and intermolecular interactions does a valine within a protein backbone…

A: Valine is an α-amino acid containing an α-amino group, an α-carboxylic acid group, and a side chain…

Q: A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48)…

A: In chromatography, we've got a go with the flow coming out of a column, when we inject a substance…

Q: Locate the peptide bond in the dipeptide shown in the balland-stick model, and identify the amino…

A: Amino acids are composed of an amino group, a carboxyl group, and an R group side chain which are…

Q: Why are salt bridges (ionic interactions) in proteins sensitive to pH?

A: Salt bridges : A salt bridge or ion bridge in electrochemistry, is a laboratory device used to…

Q: What is the approximate molecular weight of a protein with 682 amino acid residues in a single…

A: Amino acids are the building blocks for proteins/polypeptides. Amino acids are classified on the…

Q: Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the…

A: Proteins are translated from mRNA. Post translation, protein is modified and folded into secondary…

Q: Classify the fatty acid with the following structural formula in the ways indicated. COOH a. What is…

A: (a) The type designation of a fatty acid is determined by the number of unsaturations contained in…

Q: In regards to the protein structure, explain what is meant by “tertiary structure.” What are the…

A: There are four levels of protein structure are important to attain the final 3- dimensional folded…

Q: What are the Amino acids and the moieties of the following three structures?

A: The only amino acid in this compound is a phenyl alanine (enclosed within circle).

Q: What are the general characteristics of the primary, secondary, tertiary, and quaternary structure…

A: Proteins are the sequences of amino acids that are joined by peptide bond in which one amino group…

Q: Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure…

A: Proteins are made up of a long-chain of the polypeptide, which is joined by the peptide chain.

Q: Generally speaking, what two considerations determine whether a specific dihedral angle will be…

A: Answer: A dihedral angle of a protein phi (ϕ) and psi (ψ) angles is the internal angle of the…

Q: The three-dimensional structure of a protein is determined by its primary, secondary, and tertiary…

A: The order of arrangement of amino acids in the peptides is called as Primary structure. The…

Q: A protein with a known mass of 240 kDa is treated with -mercaptoethanol, a sulfhydryl reducing…

A: Proteins are polymers/chain of amino acids linked by peptide or amide bonds. It is called as primary…

Q: Classify the fatty acid with the following structural formula in the ways indicated. a. What is the…

A: Lipids  Lipids are a group of compounds that are oily or greasy in nature. They consist of alcohol…

Q: Classify the fatty acid with the following structural formula in the ways indicated. COOH a. What is…

A: Fatty acids are organic acids having hydrocarbon chains that end in a carboxylic group ( -COOH).…

Q: what are the four interactions that keep the protein structure intact?

A: Biological macromolecules are those large molecules that are necessary for the survival and growth…

Q: rotein structure and what type of bond is primarily responsible for each level?

A: Proteins are the ultimate result of a coding procedure that begins with cellular desoxyribonucleic…

Q: HiCan you help me solve this question?

A: a) Cysteine is a non-essential sulfur-containing amino acid in humans, related to cystine, Cysteine…

Q: Discuss the factors that cause denaturation and their effect on the protein structure.

A: Biomolecules are organic molecules present in living organisms. There are mainly four major…

Q: Draw Ramachandran plot for: a) regular secondary structure with Φ = 60-65 and Ψ = 60-80

A: The combination of the backbone dihedral angles ψ and ϕ statistical distribution is shown by…

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: What chemical is used for reduction of disulfur bridges in protein?

A: Disulfide bonds play a secondary role in maintaining protein structures against denaturation, they…

Q: Which of the following is TRUE? Select one: a. The disulfide bridges formed by oxidation of the…

A: The tertiary structure of the proteins is due to various interactions between the side chains in the…

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: Globular proteins are typically constructed from several layers of secondary structure, with a…

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

Q: What structural relationship is indicated by term D glucose.?

A: Monosaccharides show stereospecificity.  An asymmetric carbon is attached to four different atoms.…

Q: 57. Renaturation may be expected in the denatured proteins of which of the following cases? A.…

A: In molecular biology, renaturation refers to the restoration of a protein or nucleic acid (such as…

Q: In what type of intra and intermolecular interactions does a valine within a protein backbone…

A: Hemoglobin A is composed of two α and two β-globin chains along with the heme molecule which…

Q: What is the contribution of dilsulfide bonds in proteins?Which groups or side chain participate in…

A: The structure of the protein is crucial for its function. Primary, secondary, tertiary, and…

Q: How should one interpret the structure at these points, or proceed if these amino acids are missing?

A: Proteins are polymers of amino acids. Amino acids are amphoteric molecules as they contain…

Q: The simple average molecular weight of the  20 common amino acids is 138 , but most biochemists use…

A: The biomolecules are the basic structural and functional forms for the living system. The major…

Q: Among these amino acid combinations listed above, only the combination of Lys and Glu have side…

A: The tertiary structure of proteins are stabilized by non covalent interactions like hydrogen…

Q: The common naturally occurring form of cysteine has a chirality center that is named (R), however;…

A: Generally all other amino acids naturally found in nature in the form of S configuration with the…

Q: What are the functions of thesurprisingly large amount of unfoldedpolypeptide chain found in…

A: Protein polypeptide chains are linear polymers that are formed from a repertoire of 20 different…

Q: What is the molecular basis for the observation that the overall charge on a protein becomes…

A: Hydrogen ions, are required in various chemical and biological processes. The available level of…

Q: Draw the structural formula of the oligopeptide if the amino acids are arginine, glutamine, glycine,…

A: Proteins are nitrogenous compounds and are macrobiomolecules. They are formed of various amino acids…

Q: You are given a protein solution with a concentration of 0.15 mg/ml. Suppose that we want to prepare…

A: An analyte must be present in detectable concentrations. Depending on the requirements of the…

Q: Are all the amino-acids soluble in water? Explain why?

A: Biomolecules are organic molecules present in living organisms. There are mainly four major…

Q: Most protein dissolve in neutral salt solution, is that true? Provide reasoning

A: When the salts are added to increase the solubility of protein and dissolve protein is known as…

Q: Based on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 140 kDa and 72…

A: Protein molecules are known to exhibit different conformational structures out of them the…

Q: What are intrinsically disordered proteins ? What are their features in terms of amino acid…

A: Proteins are biomolecules composed of amino acids. Amino acids are joined together through peptide…

Q: In the tertiary structure of a protein, which pair of amino acid side chains would be most likely to…

A: Introduction: Protein are the most bountiful natural particles of the living framework. They can be…

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.