Basic chemical properties of polar positively charged amino acids in proteins. Use a few examples.
Q: Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral…
A: Introduction: Amino acids are a group of organic compounds containing two functional groups- amino…
Q: functional groups in palmitic acid, a saturated fatty acid and oleic acid, an unsaturated fatty acid
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Q: Hydrogen bonds and hydrophobic interactions play important roles in stabilizing and organizing…
A: Protein is an important biomolecule made up of small units called amino acids. These proteins are…
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A: Biomolecules that are composed of both hydrophobic and hydrophilic segments are termed amphipathic.…
Q: Describe the acid–base properties of amino acids
A: Acids provide off H+ (Hydrogen) ions in water; bases provide off OH- (Hydroxide) ions in water.…
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A: Plant storage proteins known as prolamins are known for their high proline amino acid concentration.…
Q: Creating tertiary structures of proteins involves the linking of amino acid functional groups with…
A: Proteins are the building blocks of the body. All the life forms consist of proteins in their cell…
Q: All of the following are considered weak interactions in proteins, except:
A: Proteins are the macromolecules composed of amino acids bound together by peptide bond between amino…
Q: structure of valine at pH of 12
A: An amino acid is fully protonated at low pH, as the pH increases more than pKa of an ionizable…
Q: Briefly describe how monosaccharides like glucose and fructose assume or transform into its…
A: It is asked to briefly describe how monosaccharides like glucose and fructose assume or transform…
Q: Amino acids are the building blocks for proteins in the cell. The structures of the amino acids…
A: Chiral centers refers to the Carbon at which 4 different groups are attached. It contains four…
Q: What special purpose methionine serves
A: Methionine is referred to as an amino acid comprises of the sulphur group responsible for forming…
Q: One round of Edman degradation of the peptide: H2N- Gly-Arg-Lys- Phe-Asp- COOH which of the…
A: The given peptide has four residues names as glycine, arginine, lysine, phenylalanine and aspartic…
Q: Bradykinin, a peptide that helps to regulate blood pressure, has the primary structure…
A: Bradykinin is a peptide found in the body, which helps control inflammation.
Q: Name and discuss the non-covalent interactions that maintain protein structure.
A: Several noncovalent interactions stabilize the three dimensional structure of a protein and hence…
Q: Basic chemical properties of amino acids with aromatic radicals in proteins. Use a few examples.
A: The aromatic amino acids found in protein are phenylalanine, tyrosine, and tryptophan. Phenylalanine…
Q: Basic chemical properties of non-polar (hydrophobic) amino acids in proteins. Use a few examples.
A: Amino acids are the building blocks of the protein. whose backbone consists of carboxyl group…
Q: Basic chemical properties of polar negatively charged amino acids in proteins. Use a few examples
A: Amino acids are precursors of proteins which undergo condensation reaction to form peptide bonds…
Q: Because of their tendency to avoid water, nonpolar aminoacids play an important role in forming and…
A: Polymers of L-alpha amino acids form the protein.The structural organisation of protein can be…
Q: Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral…
A: There are about twenty essential and nonessential amino acids are often present in proteins. Amino…
Q: Using octahedral symmetry, match each ligand SALC with its most likely interaction with a meta…
A:
Q: Comment on why the feature ~210 nm in Circular Dichroism and Infrared spectroscopy is useful for…
A: Circular dichroism spectroscopy (CD) is a fundamental insightful method used to investigate…
Q: Draw peptide Pro-Ser-Ala-Phe-Glu as you would see it at pH 7. Include stereochemistry.
A: Proteins are made of different amino acids joined through peptide bonds. The amino acids are…
Q: peptide in a solution with a pH of 7 has the following sequence: K-R-E-D-H-D-E…
A: The isoelectric point (pI) is the value of pH at which molecule carries no charge or the net charge…
Q: Suggest a reason why trans fatty acids have melting points similar to analogous saturated fatty…
A: Fatty acids are considered as the long hydrocarbon chain of the carboxylic acid of lipids or fats.
Q: Why picric and tannic acid is used for the treatments of burn. Explain this in the concept of…
A: Tannic acid and picric acids are phenolic compounds. These are water-soluble compounds…
Q: Contribution of the features of the alpha-helix to the stability of the protein.
A: Protein play wide variety of essential function in our body. They provide strength and structural…
Q: The general structure of all amino acids are same except for ___________
A: Amino acids are organic compounds having two functional groups namely carboxyl and amino group. Some…
Q: Calculate the isoelectric point of Aspartic acid
A: The isoelectric point of a solution is defined as the pH value at which amino acid or peptide is…
Q: Acid hydrolysis of polypeptides may lead to complete destruction of tyrosine residues.
A: Proteins and peptides are macromolecules made up of covalently bonded amino acid residues in linear…
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Q: Sketch resonance structures for the peptide group.
A: Peptides are short-chain made up of amino acids. The amino acids are linked together through peptide…
Q: Which of these statements about the tertiary structure of a polypeptide is(are) untrue? You may…
A: Protein play wide variety of essential function in our body. They provide strength and structural…
Q: Name another condition besides heat and exposure to a bond disruptor (like alcohol) that could…
A: Proteins are biomolecules composed of Amino acids. Proteins have different levels of structural…
Q: Protein Structure Describe the four levels of protein structure: Primary, secondary, tertiary, and…
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Q: Amino acid polymers consisting of more than 50 amino acids are called _____________.
A: Amino acids are building blocks of proteins where each residual was joined by a covalent bond.…
Q: Hydrophobic intercation associated with protein tertiary structure involve
A: Hydrophobic interactions are the type of interactions between water and hydrophobic molecules (low…
Q: difference between partially hydrolyzed protein and completely hydrolyzed protein
A: Proteins are biomolecules made up of long chains of amino acids linked by a peptide bond which serve…
Q: What types of interactions are possible between the side chains of the polypeptide shown below?…
A: Amino acids side chains form H-bonds when amine and carboxylic groups are present in the side…
Q: Discuss and compare the potential contributions for tertiary structure in a protein for the side…
A: Amino acids are basic subunits of proteins. Alpha carbon of amino acids consist of side chain group,…
Q: Does the location of the -OH group in a monosaccharide affect its function/bioactivity? Why or why…
A: There two types of anomers in a monosaccharide. Alpha and beta anomers, the C1 atom of the carbon…
Q: Basic chemical properties of polar uncharged amino acids in proteins. Use a few examples
A: Amino acids are building blocks of proteins, whose backbone consist of amino group (NH2), carboxyl…
Q: Explain why it is difficult to draw conclusions about the conformational changes of a protein based…
A: A polypeptide protein is made of an amino acid chain, all amino acids are or different properties…
Q: Interactions that make up the three-dimensional structure in proteins.
A: Amino acids Proteins are the polymers of nitrogenous compounds called amino acids. Each amino acid…
Q: Amino acid isomerism (name types). Isomerism of the carbon skeleton of amino acids - give a few…
A: Isomerism: Isomerism is the phenomenon in which two chemical compounds have the same molecular…
Q: What is amphoterism? Show using chemical equations the amphoteric property of protein.
A: Proteins are one of the major biomolecules. It is made up of building blocks called amino acids.…
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- Explain briefly why the ionizable properties of amino acids are so crucial in the structure and function of proteins.Proline provides structural regidity in proteins. What is the consequence of this on protein structure?Explain why it is difficult to draw conclusions about the conformational changes of a protein based on a single crystal structure.
- A protein’s shape depends partly on electrical attractions between charged or polarized groups in various regions of the protein. True or false?Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?the membrane solubility of a steroid is higher than the membrane solubility of a carbohydrate true or false?