Why do some ordered proteins require molecular chaperones to fold into their active conformations, whereas others do not?

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: Many of the loops on proteins are composed of hydrophilic amino acids. Why might this be the case?

A: Protein is one of the important biomolecules. This protein is made up of sequence amino acids which…

Q: To what category does this amino acid belong? Note that the non-ionized form is shown! H H. N-C-C он…

A: Depending on the properties of the R-group amino acids get classified into different categories,…

Q: How can the phosphorylation of a protein result in conformational changes?

A: Phosphorylation generally alters the structural as well as functionality of protein. It alters the…

Q: The three-dimensional structure of biomolecules is more conserved evolutionarily than is sequence.…

A: Biomolecule also called biological molecule is any numerous substances that are produced by cells…

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: Once modified, do proteins always have the correct threedimensional structure?

A: Protein modification is important to attain the specific shape of the protein, which is crucial for…

Q: Why is it important to identify the N-terminal residue(s) of a protein?

A: Protein is composed of a long chain of amino acids, which are joined by a peptide bond. These…

Q: Phosphorylation is a common covalent modification of proteins in all forms of life, which leads to…

A: Phosphorylation refers to the biochemical process that involves the addition of phosphate to an…

Q: Why do some amino acids have charges while some do not?

A: Amino acids have an amino group, an acid group, and an organic R group. The R group is referred to…

Q: How Is the Primary Structure of a ProteinDetermined?

A: The proteins are synthesized from the mRNA which carries the genetic information of the DNA. These…

Q: How does a protein make the transition from an unfolded structure to a unique conformation in the…

A: The conformation in which a molecule is active biologically is known as native conformation. The…

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: Why are multifunctional proteins necessary and/ordesirable?

A: Proteins are composed of a long chain of amino acid, which is bonded by the peptide bond. This…

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: Most proteins contain more than 100 amino acid residues. If you decided to synthesize a “100-mer,”…

A: Protein is a macronutrient that is essential to building muscle mass.

Q: How many ways can four different amino acids be arranged in a peptide so that each peptide is…

A: Amino acids are organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups,…

Q: Which is the major force responsible for the formation of an α-helix in protein secondary structure?

A: Peptides are formed by reacting the carboxyl group of one amino acid with an amino group of another…

Q: The simplest form of the Ramachandran diagram is calculated by ignoring hydrogen bonding,…

A: The Ramachandran plot is a plot of the torsional angles - phi (φ)and psi (ψ) - of the residues…

Q: Why do the pK values of ionizable groups differ between free amino acids and amino acid residues in…

A: The acid dissociation constant (Ka) is the quantitative measure of the strength of an acid or amino…

Q: Which amino acid replacement would result in the biggest structural change in a protein if a Cys…

A: Amino Acids Introduction Proteins are polymers made up of nitrogenous chemicals known as amino…

Q: Is it expected that a change in the primary, in the secondary or in the tertiary structure of a…

A: The primary level of protein structure determines the sequence of amino acids in the polypeptide…

Q: What is the importance of the –R group (variable radical) in an amino acid molecule?

A: Amino acids are compound containing amino group, carboxyl group and a variable R group.  R group is…

Q: How Do Protein Subunits Interact at the QuaternaryLevel of Protein Structure?

A: Living organisms contain four types of macromolecules, carbohydrates, proteins, nucleic acids, and…

Q: Shown below is a portion of primary sequence of a very large protein.…

A: The protein's overall structure contains both alpha helices and beta sheets. The folding and…

Q: In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in…

A: Sickle cell disease is a blood condition that is most commonly found in the people of African…

Q: Why are binding sites in proteins often located at interdomain boundaries?

A: Binding site is a position on a protein which binds to an incoming molecule that is smaller in size…

Q: What is the concepts of the native conformation of proteins? Why and how do proteins refold and…

A: Proteins are polypeptide structures consisting of one or more long-chain amino acid residues. They…

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 sample of the amino acid tyrosine is barely soluble in water. Would a polypeptide containing only…

A: Tyrosine is one of the 20 standard amino acids that are used by calls to synthesize proteins. It is…

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: Which of the following peptides will likely form a loop or turn in a protein and explain why

A: The turns are the third type of secondary structure. These are short, U-shaped secondary structures,…

Q: Consider the peptides Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser. How do these two peptides differ?

A: Introduction: The organic molecules that contain two functional group that is amino and carboxyl are…

Q: Many eukaryotic enzymes, such as fatty acid synthase, are multifunctional proteins with multiple…

A: multifunctional enzymes are those enzymes in which there are two or more active sites.

Q: _____________ are degrons with sequences containing proline, glutamate, serine, and threonine…

A: Peptides are chain of amino acids containing few amino acids. The amino acids are attached with…

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: What type of intramolecular interactions can be found between amino acids within proteins to help…

A: Polymers of L-alpha amino acids form the protein. The structural organisation of protein can be…

Q: What is the tertiary structure of a protein? What are the main types of tertiary structure?

A: Proteins are the large size macromolecules that are formed by the polymers of amino acids,…

Q: Four of the most abundant amino acids in proteins are leucine, alanine, glycine, and valine. What do…

A: Amino acids are the building blocks of proteins. these are the organic components when proteins are…

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: 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: If you were to design a small peptide with a large net positive charge at physiological pH, which…

A: The peptide is a small amino acid sequence where the alpha carboxylic group of one amino acid is…

Q: Why do some proteins require molecular chaperones to foldinto their active conformations, whereas…

A: Protein folding is a process by which a polypeptide chain folds to become a biologically active…

Q: Which R group would most likely be found in a hydrophobic area of the tertiary structure of a…

A: The protein attains a specific conformation for performing mature protein functions in the body.

Q: How does the primary structure of a protein corresponds to the linear order of amino acids in a…

A: Proteins are composed of amino acids. Natural proteins which get synthesized inside the cells are…

Nucleotides

It is an organic molecule made up of three basic components- a nitrogenous base, phosphate,and pentose sugar. The nucleotides are important for metabolic reactions andthe formation of DNA (deoxyribonucleic acid) and RNA (ribonucleic acid). 

Nucleic Acids

Nucleic acids are essential biomolecules present in prokaryotic and eukaryotic cells and viruses. They carry the genetic information for the synthesis of proteins and cellular replication. The nucleic acids are of two types: deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). The structure of all proteins and ultimately every biomolecule and cellular component is a product of information encoded in the sequence of nucleic acids. Parts of a DNA molecule containing the information needed to synthesize a protein or an RNA are genes. Nucleic acids can store and transmit genetic information from one generation to the next, fundamental to any life form.