In what type of intra and intermolecular interactions does a valine within a protein backbone typically participate? How would this variation in Sickle Cell Disease be classified?

Q: How is the activity of an allosteric protein modulated?

A: Proteins are the building blocks of cells and play crucial role in physiology due to the involvement…

Q: is amino acid 213 in 1mry is THR ?

A: 1MRY crystal structure represents the structure of the akt2 kinase domain. It belongs to a…

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: Are amino acids other than the usual 20 amino acidsfound in proteins? If so, how are such amino…

A: Amino acids, the chiral carbon-containing molecules that form the monomer of peptides or proteins in…

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: What distinguishes d-amino acids from lamino acids? What biological functions do peptides containing…

A: Amino acids are organic molecules, which act as the building blocks of proteins. Amino acids are…

Q: Which kinds of interactions can be seen in the tertiary structure of proteins?

A: The determination of biological function of a protein lies in its conformation or 3D structure.…

Q: 19.40 Indicate whether each of the following statements describes the primary, secondary, tertiary,…

A: We are authorized to answer one question at a time since you have not mentioned which question you…

Q: Are the enzyme ADH and ALDH simple or conjugated proteins, and how do you know this?

A: ENZYMES- Enzymes are highly specialized proteins that act as a catalyst in the biological system,…

Q: why would one missing amino acid make a difference in the protein's shape, and why would a change in…

A: Amino acids are the building blocks of proteins and they are arranged in a particular shape to…

Q: Are the amino acid residues at the active site need to be in close proximity to one another…

A: Enzymes are the catalysts that catalyze biochemical reactions. These are proteinaceous in nature as…

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: How does the structure of the protein in the aggregated form differ from that of the protein in its…

A: The protein which is responsible for the neuro-degenerative disease is PrPpc (prion protein).

Q: Explain about  the Iodine (Protein Bound Iodine) ?

A: Iodine is a mineral that is naturally found in the earth. It is purple-black in color. It is an…

Q: What kinds of changes take place in a protein when it is denatured?

A: Denaturation is a process in which a protein loose the quaternary structure, tertiary structure, and…

Q: Hemoglobin is a tetramer consisting of two a and two b chains. What level of protein structure is…

A: Hemoglobin is a globular protein that is involved in transporting oxygen from the lungs to tissues…

Q: Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below.…

A: Since you have posted a question with multiple sub-parts, we will solve first three sub- parts for…

Q: Globular proteins are water-soluble, whereas fibrous proteins are insoluble in water. Indicate…

A: the nature of amino acid present on a protein or a cell surface depends on the nature of the cell .

Q: How does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein…

A: Expecting that you know the primary, secondary, tertiary and quaternary structure of a protein.…

Q: The interactions between the 2 a and 2 b subunits of hemoglobin represent what type of protein…

A: Protein structure: The three dimensional arrangement of monomer units of protein constitute the…

Q: What conditions are required for disulfide bonds to form between cysteine residues in a protein?

A: Cysteine is polar amino acid, the side chain have a thiol (-SH) functional group.

Q: Give an example of a protein containing primarily betapleated sheets. Is this a fibrous or globular…

A: Protein structure decides the amino acid sequence, chemical bonds found between atoms in the…

Q: Which of the following would be considered an incomplete protein?

A: Proteins are macronutrients needed for tissue growth and repair, digestion, immunity, and…

Q: What type of protein is included in milk? When milk sourness occurs, why does this protein…

A: Proteins are a linear chain of amino acid sequences attached together via peptide bonds. Proteins…

Q: Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below.…

A: "Since you have asked multiple questions, we will resolve the first question for you. If you want a…

Q: A protein with a quaternary structure is a multidomain protein. Is this always correct? Explain.

A: Proteins are polypeptides consisting of unbranched polymers constructed from 22 standard α-amino…

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: Hemoglobin is composed of which two types of polypeptide chains, alpha?

A: Hemoglobin (Hb) has a significance in oxygen transport from the lungs.

Q: Are peptide bonds free to rotate in folded protein? Can they be ionized at extreme pH values?

A: Proteins are composed of the linear chain of amino acid sequences attached together via peptide…

Q: Give an example of a protein containing primarily alphahelices. Is this a fibrous or globular…

A: α-helix structure of a protein is a secondary structure of proteins where it forms a hydrogen bond…

Q: crystals of deoxy Hb are exposed to air,

A: The red pigment exclusively found in erythrocytes is known as Hemoglobin (Hb).  The normal…

Q: Describe the effect of the amino acid change on protein function: how does the HbS protein function…

A: Proteins are the polymers of amino acids. These amino acids are linked together by peptide bond. Now…

Q: Which noncovalent interactions (discussed in Section 8.2) are responsible for the cohesion of lipid…

A: Lipids are organic molecules made of hydrogen, carbon, and oxygen that serve as the structural and…

Q: The following sequence of amino acids are part of adult hemoglobin from the N-terminus. DRAW THE…

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

Q: List three purposes served by protein turnover.

A: Proteins are composed of amino acids. An amino acid consists of an amino group (-NH2), a carboxylic…

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: Disulfide linkages are uncommon in cytoplasmic proteins, whereas they are common in extracellular…

A: Oxidation is the most common way for disulfide bonds to form in the endoplasmic reticulum.

Q: Name another condition besides heat and exposure to a bond disruptor (like alcohol) that could…

A: Proteins are polymers that are made up of monomers called amino acids. An amino acid has a central…

Q: Which level of protein structure organization are lost hydrolysis and denaturation?

A: Protein: The macromolecule is made up of long chains of amino acids that are connected through…

Q: A major interaction that stabilize tertiary structures of proteins is

A: Protein play wide variety of essential function in our body. They provide strength and structural…

Q: What intermolecular forces hold protein subunits in a quaternary structure?

A: The protein's quaternary structure is the association of several protein chains or substituents into…

Q: . Theoretical and experimental measurements show that in many cases, the contributions of ionic and…

A: The amino acid sequence of the polypeptide/protein is the primary structure of the protein. The…

Q: Translate the following amino acid sequence into one-letter code:…

A: The unique one-letter code was developed for easy and fast recognition of amino acids. Each of the…

Q: What is the binding between two amino acids called?

A: Protein is a polymer formed from amino acid joined by peptide bond. It is abundantly found in the…

Q: Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this…

A: Amino acids are biomolecules with an alpha carbon bonded to 4 valencies. The valencies(groups) are a…

Q: What structural features of proteins mark them for destruction?

A: Structural features:      Proteins are the power-pack of the cell. Over molecular basis, whatever…

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…

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.