Proteins are damaged for a number of reasons.

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

A: Enzymes are proteins that go about as natural impetuses. Catalysts speed up substance responses. The…

Q: Explain how in some cases a single nucleotide change in a DNA sequence can have very detrimental…

A: Mutations is the sudden heritable change in the make up of gene. Mutation basically occur by…

Q: Define ligand

A: Biological molecules that are present in living organisms and are involved in various biological…

Q: Differentiate the stepwise stages in protein folding.

A: Protein folding: a. Proteins are composed of amino acid chains that obtain their biological and…

Q: All three types of biopolymers are set from the building blocks with similar types of chemical…

A: Proteins are polymers of amino acids attached through peptide bonds. Proteins have four different…

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: When the voltage gated potassium channel moves from an open to a closed formation the 5th alpha…

A: Biomolecules are the biological molecules that are present inside the living organisms. These…

Q: What characteristics of a binding site determine its affinity for a ligand?

A: The binding site is a region where the upcoming molecule like any ligand/substrate (smaller in size)…

Q: For a protein that binds multiple ligands with negative cooperativity, which of the following is…

A: The ligand binds to its target molecule

Q: Provide some instances of simple physiologically active peptides.

A: Biological molecules are the molecule present in the body that participate in various metabolic…

Q: Define binding affinity

A: Binding affinity is conjointly measured as a part of the drug discovery method to assist design…

Q: Describe in no more than ten sentences the four levels of protein structure, and cite the…

A: Proteins are composed polypeptide chain, which is bonded with the peptide bond.

Q: Explain the relationship between protein folding andprotein function.

A: Protein structure is a three-dimensional conformation. The protein folding occurs in four levels and…

Q: Protein denaturation is the disruption of a protein's secondary to quaternary structures. Protein…

A: When the proteins are exposed to some acids, base, or inorganic solvent they tend to lose their…

Q: Explain how a chaperone protein works

A: Protein folding is a process of aggregation of amino acid chain or polypeptide chain into a primary…

Q: What are three purposes served by protein turnover?

A: Protein is a building block of the body. A majority of the cellular components are made up of…

Q: All proteins have primary (1°), secondary (2°) and tertiary (3°) structure. In addition, some (but…

A: Proteins are the polypeptides in which amino acids form the building blocks. Proteins are important…

Q: β-mercaptoethanol ____, and urea _____ disrupt the interactions involved in formation of α-helices.…

A: DNA stands for deoxyribonucleic acid. It is the genetic material of the organisms that transfer from…

Q: Describe the function of tRNA in protein assembly.

A: The cells are the basic biological structural and functional units of life. The genome of an…

Q: List three important distinctions between fibrous and globular proteins.

A: Fibrous proteins and globular proteins are the two primary types of the protein's tertiary…

Q: Adenosine triphosphate is an imortant molecule becauseit

A: Electron transport chain is mechanism which takes the electrons from the electron donor and gives to…

Q: Explain Modular nature of protein domains.

A: Eukaryotic proteins are standard in nature. several macromolecules contain severally folding…

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: Explain why heat, pH changes, and other environmental changes can interfere with a protein's…

A: Proteins are complex molecules with many vital functions in living organisms. The sequence of amino…

Q: (9 Why does DNA contain thymine instead of uracil? Justify.

A: Given: DNA contain Thymine instead of Uracil. DNA is a long polymer of polynucleotide chain. It…

Q: Some proteins are shuttled back and forth between the nucleus and the cytoplasm.  How do you think…

A: Nuclear envelop found in the cells, separates the contents of nucleus from cytoplasm and also…

Q: Explain how single nucleotide changes can have mostly different effects on protein function.

A: Genetic material is nothing but the sequence of nucleic acids which is called as DNA. It contains…

Q: At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein…

A: Proteins are large-sized heteropolymeric macromolecules having two or more polypeptide chains. They…

Q: Define The domain structure of cytoplasmic dynein.

A: Dynein is a motor protein that requires ATP as a source of energy to mediate intracellular…

Q: Describe the structure and functions of deoxyribonucleic acid (DNA), ribonucleic acid (RNA), and…

A: DNA is genetic material present in each and every cell. It stores all the structural, functional and…

Q: Provide three examples of medical applications of proteins.

A: Proteins are the biomolecules which are made up of Amino acids linked Together by peptide bonds.…

Q: proteins

A: Protein synthesis: The proteins are made of a long chain of amino acids which are coded by DNA. The…

Q: Explain how mutations can af

A: Proteins are macromolecules or large biomolecules, which comprise one or multiple chains of amino…