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: 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 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: Define mis-sense mutation and non-sense mutation.

A: Changes or alteration in DNA  that results in some altered expression is known as mutation.

Q: Define binding affinity

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

Q: Define protein complexes

A: the structure of a molecule dictates its function. This essay describes the importance of the shapes…

Q: What is the essential condition for a protein to be identical to another protein?

A: In biochemistry, proteins are defined as the macro-biomolecules that are formed from a linear chain…

Q: Identify how mutations influence protein structure.

A: The mutation is the alteration in gene by causing disruption in the nucleotide sequence. It can be…

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: Describe several functions of polypeptides.

A: Polypeptides are will make up the protein by joining amino acids together by a peptide bond.…

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: 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: 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: conditions affect the structure of a protein?

A: The stability of the protein is determined by the various weak interaction and thermodynamics .…

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: List the four characteristics of a protein-binding site?

A: Proteins are the polymers of amino acids.

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…

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

A: An allosteric protein has a binding site for a ligand and an allosteric site for a regulatory…

Q: Discuss the general mechanisms by which proteins are precipitated.

A: Proteins are the unbranched heteropolymer of the amino acids. Proteins have different types of…

Q: An intermediate folding stage seen in protein denaturation or renaturation is called?

A: Proteins exist in four levels of molecular conformations in a human body: primary, secondary,…

Q: Mention any four important characteristics of genetic code.

A: The DNA is the genetic material that is passed from one generation to the next generation. It is…

Q: Define Biological Value (BV) of Proteins

A: Protein is a macronutrient biomolecule that is essential to building muscle mass. It is commonly…

Q: Describe protein denaturation and its effects

A: Proteins are the building blocks of the body. It plays an essential role in the body. Proteins are…

Q: Proteins associate with membranes in a number of different ways. identify them and outline their…

A: Cell membrane is composed of a phospholipid bilayer that is associated with different proteins…

Q: What functions does protein form?

A: proteins are complex and large molecules formed by the combination of a group of smaller amino acid…

Q: A protein is likely to become a denatured when?

A: Proteins are amino acids residues joined together by peptide bonds , which form extremely complex…

Q: Describe the  Stages in the formation of a functioning protein in the nucleic acid.

A: Nucleic acid DNA and RNA are polymers of nucleotides.