In some cases, a single amino acid substitution can cause a protein to lose its biological activity. In other cases, a single amino acid substitution causes no change to a protein's biological activity. Which statement can best be used as evidence to support an explanation for these observations?
Q: Which
A: Presence of amino acids and its proximity affects pka value of other
Q: List two types of DNA mutations and state which one is more likely to have a severe effect on the…
A: DNA mutations are a sudden change in the DNA sequence. Mutations can be caused by various factors,…
Q: If a particular 180 amino acid polypeptide is known to sample 3 preferred states as it folds into…
A: Anfinsen's experiment showed that the protein is intrinsically capable of finding its lowest-energy…
Q: Which of the following is a drawback of using base hydrolysis during amino acid composition? O…
A: A protein is consisted of several amino acids bond together in sequence with peptide bond. To…
Q: Explain with examples why qualitative and quantitative analyzes of amino acids are important.
A: The qualitative analysis of amino acids is marked by color change, precipitation, ring formation,…
Q: Solve the attached problem
A: Introduction: Amino acids are the natural molecule that contain two functional group that is amine…
Q: Which of the following combination is are non-essential amino acids? A. Leucine and Isoleucine…
A: Proteins are polymers of amino acids, which suggests proteins are made from amino acids. Amino acids…
Q: Even if a protein has the majority of its amino acids different than another, it is possible for…
A: Biological macromolecules are those large molecules that are necessary for the survival and growth…
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: how do we maintain a steady support of amino acids in the body?
A: Amino acids are the basic units of proteins and proteins are very important for our body because…
Q: The effect of base-pair substitution mutations on protein function varies widely from no detectable…
A: It is because of the protein functionality isn't affected by the mutations occurred in the intron…
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: What property is exhibited by proteins which allows them to absorb large quantities of water?…
A: Proteins are organic molecules composed of amino acids. The polar nature of proteins makes them…
Q: Explain how it is feasible to modify an amino acid inside a protein without affecting its function.
A: Proteins are one of the body's most significant macromolecules. These are made up of amino acids…
Q: List down which amino acids are capable of the following interactions in the tertiary structures of…
A: There are 20 standard amino acids are there which make up all the proteins inside the cell. Amino…
Q: A protease is an enzyme that catalyzes the hydrolysis of the peptide bonds of target proteins. How…
A: A peptide bond is an amide type of covalent chemical bond linking two consecutive alpha amino acids…
Q: Which of the following amino acids is not part of tetramer that is bounded to NAM and glycine?…
A: Peptidoglycan is the major component of bacterial cell wall. Gram positive bacteria have a thick…
Q: If a Cys residue in a protein was replaced with either Ser or Phe amino acid, which substitution…
A: Amino acids Proteins are the polymers of nitrogenous compounds called amino acids. Each amino acid…
Q: Which of the following correctly describes the 3 amino acids that are most likely to undergo…
A: Amino acids are organic compounds composed of carbon, hydrogen, oxygen, and nitrogen. They are the…
Q: The change of one conformation of protein to another is called a. allosteric transversion b.…
A: Option b Allosteric transition
Q: does all 20 amino acids soluble in organic solvents like acetone and chloroform? true or false
A: The monomeric unit of a polypeptide is amino acids. These are joined by a peptide bond to form these…
Q: Which of the following is an example of protein denaturation? * A. Amino acids fold into…
A: The proteins are folded into their three dimensional structure via four levels of organizations :…
Q: Why do some genetic mutations lead to completely nonfunctional proteins while others do not affect…
A: A mutation is a sudden change in the sequence of DNA. DNA is made up of nucleotides. DNA is…
Q: Which of the following statements about amino acids is/are incorrect? I. The formation of a…
A: Amino acids make up proteins. Amino acids are joined to each other by peptide bonds. There are about…
Q: One of the following is false: a. Glycosylated HbA has glucose attached to N- terminal of beta…
A: HbA, also termed as adult hemoglobin, is the common hemoglobin tetramer found in humans. This…
Q: Draw a generic amino acid and identify its α carbon and its substituents.
A: An amino acid is the organic compound which contains a carboxyl group, an amino group, hydrogen…
Q: Is the statement: "There is energy requirement for every amino acid added in a growing polypeptide…
A: Amino acids are the building blocks of proteins. The synthesis of polypeptide chain occur during…
Q: N-linked oligosaccharides can be covalently linked to proteins at which amino acid? a. Gly b.…
A: Glycoproteins are known as specialized proteins that are composed of oligosaccharide chains i.e,…
Q: In a disease known as phenylketonuria, a person is not able to break down the particular amino acid…
A: Phenylketonuria: Phenylketonuria (also referred as “PKU”) is a unique genetic condition that causes…
Q: Does a mutation always result in a change of an amino acid sequence in protein? Why?
A: A mutation is the alteration of the nucleotide sequence of the genome which may or may not result in…
Q: Which amino acid metabolism is affected in Alkaptonuria? a. Phenylalanine b. Histidine c.…
A: Alkaptonuria : Autosomal recessive disorder caused by homogentisate 1,2-dioxygenase enzyme…
Q: Why is an amino acid called a “Residue” and not just: “amino acid” in a protein
A: Amino acids are the compounds which are composed by an amino group ,a carboxyl group ,a hydrogen…
Q: How does the degree of unsaturation and structure of fats affects its functionality, for example in…
A: Fats are essential macronutrients. There are several forms of dietary fat, and some are far more…
Q: To examine: Whether the statement "Loops of polypeptide that protrude from the surface of a protein…
A: Proteins are essential dietary components. It is made up of a polypeptide chain, which is a chain of…
Q: The link between gene and protein was first articulated by Beadle & Tatum, who proposed the…
A: Gene is a structural and functional unit of DNA which contains the genetic information needed for…
Q: The biological marcomolecules composed or multiple units of amino acids is
A: Molecules that are organic in nature and are required by our body to maintain the health of the…
Q: Amino acids have the same basic chemical backbone, with an __________ group on one end and an…
A: Amino acids are the monomer units which condese to form proteins . They are held together via…
Q: All are both ketogenic and glucogenic amino acids except Group of answer choices Tyrosine Arginine…
A: Gluconeogenesis is the process by which some amino acids can be converted into glucose. As a step in…
Q: During the folding of a protein in a buffered aqueous solution, what happens to the entropy of the…
A:
Q: What factors affect denaturation and refolding of proteins
A: Denaturation(unfolding) is the process in which protein loses the three-dimensional structure by…
Q: Can a mutation change a protein’s tertiary structure without changing its primary structure? Explain…
A: Every function in living beings depends on proteins. There are different types of proteins and each…
Q: Which types of amino acids (polar, nonpolar, or charged) are expected to be found primarily in the…
A: On the basis of shape and solubility proteins are classified as: Globular proteins Fibrous protein…
Q: does it mean for a protein to be denatured
A: Protein denatured means the activity of protein has been changed or stop by changing in protein…
Q: Which one of the following pairs are semi-essential amino acids for humans? A. Histidine and…
A: Introduction: The correct choice is option C. Arginine and Histidine
Q: Which of the following amino acids contains a carboxamide side chain? A.glutamine B.alanine…
A:
Q: There is energy requirement for every amino acid added in a growing polypeptide chain. Is this true…
A: Introduction: The information transferred from DNA to messenger RNA (mRNA) is translated into an…
Q: Which of the statements about denaturation are true? Protein denaturation involves cleavage of its…
A: Denaturation of proteins refers to the breaking of non-covalent bond and disulfide bond resulting in…
please see attached
Step by step
Solved in 2 steps
- Which of the following most directly applies to the formation of the secondary structures of proteins? A B с D formation of ionic bonds between the R groups of two polypeptides formation of nonpolar interactions between two R groups on the same polypeptide formation of covalent bonds via dehydration reactions between two amino acids formation of hydrogen bonds between between amino and carboxyl groupsShown below are three amino acids: H,N-CH-C-o ҫн, H,N-CH-C-o CH, H,N-CH-C-o ČH, Tyrosine Tyr Y Phenylalanine Phe F Alanine Ala A 1. Which amino acid is the least hydrophobic? 2. Which amino acid is most hydrophobic? 3. Which amino acid is intermediate? 4. Explain why (2) is more hydrophobic than (3). 5. Explain why (3) is more hydrophobic than (1).When a protein folds into a quaternary structure the outside amino acids are exposed to the aqueous (water rich) environment. These amino acid R likely have what chemical properties? O The amino acid R groups are polar and hydrophilic The amino acid R groups are non-polar and hydrophobic O The amino acid R groups have hydrocarbon functional groups O The amino acid R groups have unreactive functional groups
- The chemical structures of the two opposing ends in any polypeptide chain are different because: O a. the structures of the chemical groups that create the polypeptide backbone differ from each other in any polypeptide chain O b. the positively and negatively charged amino acid side chains carry different electric charges in any polypeptide chain O c. the chemical structures of the polar uncharged and nonpolar amino acid side chains differ from each other in any polypeptide chain O d. the positively and negatively charged amino acid side chains form electrostatic interactions with each other in any polypeptide chainTertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrectName four major groups of amino acids, categorizedby the properties of their R groups. Explain how thechemical properties of each group affect protein shape.
- Researchers investigating the protein composition in mice have identified a new protein and found evidence of sulfur-containing cysteine at regular intervals in its primary structure. Which of the following best describes the most direct significance of this finding? A B с D The secondary structure of the protein will include tightly would alpha-helices but no beta sheets. The tertiary structure of the protein likely contains a relatively high number of bends and angles. The protein will form a relatively highly stable tertiary structure. The dietary intake of mice must include the regular ingestion of cysteine.Which of the following statements concerning the peptide NH3*-Val-Ala-Gly-Lys-Leu-Gly-Val-Phe- Tyr-lle-COOH is correct? O The peptide can form an alpha-helical secondary structure O The peptide can form a beta-pleated sheet O The last amino acid residue is Val. O Three peptide linkages are present.the sequence of amino acids in a protein is known as the secondary structure true or false?
- Draw the two amino acids serine and alanine, and a dipeptide that could be formed by combining these two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature the amino terminus is on the left and the carboxyl terminus is on the right. 1. How many waters were released by formation of this dipeptide from individual amino acids? [ Select ] 2. How many hydrogen bond donors does your dipeptide have? [ Select ] 3. If you were to draw this dipeptide at a pH :1, would the number of hydrogen bond donors change? [ Select ]29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.57Draw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0 backbone of glutamic acid. 2. Ionic bond- between ionized aspartic and asparagine amino acids. 3. Disulfide interaction between 2 molecules of Cysteine amino acids. 4. Hydrophobic interaction between Alanine and Leucine R-groups.