When electrons are removed from a food molecule,the moleculeis conducting anendergonic reaction. reduced. oxidized. inequilibrium. polymerize

Q: Please provide explanations and work for each part of the question. If able to keep the same format…

A: Protein structure is a fundamental concept within biochemistry, encompassing the hierarchical…

Q: 7. How many liters of a mouthwash can be prepared from 100 mL of cinnamon flavor if its…

A: To prepare a mouthwash with a concentration of 0.5% (v/v) cinnamon flavor, you need to calculate how…

Q: In the presence of oxygen, most living cells make ATP by oxidative phosphorylation, which takes…

A: a.the given chemical equation is-                                                         An…

Q: The strength of collagen comes from which of the following?   a. hydrophobic interactions and…

A: Collagen is a protein found in connective tissues like tendons, cartilage, organic matrix of bone…

Q: What is the difference in atp formation in glycolysis and o inactive metabolism

A: Glycolysis is a metabolic pathway that occurs in the cytoplasm of cells. It breaks down one molecule…

Q: What would spread (fragmented) bands in the electrophoresis gel tell you about the quality of your…

A: Gel electrophoresis is a technique used to separate DNA fragments according to their size. The DNA…

Q: Mary Jo prepared a series of diluted samples by taking 1 mL of sample and adding it to 4 mLs of…

A: Here, Mary Jo is undertaking serial dilution (i.e. a series of consecutive dilutions) comprising of…

Q: calculate the pI for tripeptide R-H-D

A: The pH of a solution at which a protein's net charge equals zero is called the isoelectric point…

Q: What is the net charge of cysteine in an aqueous solution at pH 9? Carboxyl group pKa = 1.92; Amino…

A: Cysteine is a polar but uncharged amino acid with thiol side group. The cysteine side group is…

Q: pH > 7 in the lungs results in O deprotonating of histidine, making it neutral. Oprotonating of…

A: The pH, which stands for "potential of hydrogen," is a measure of the acidity or alkalinity of a…

Q: 1. The following reactions can be coupled in the citrate cycle. kJ/mol kJ/mol Succinyl-CoA GDP + Pi.…

A: The Krebs cycle also known as the TCA cycle (tricarboxylic acid cycle) or Citric acid cycle. This…

Q: From the peptide chain: Met-Tyr-Phe-Arg-Ile-Glu-Asn-Asp-Ser, draw the structure of the product…

A: There are four types of biological macromolecules: proteins, nucleic acids, lipids and…

Q: The place on the enzyme where the substrate binds is called the: a) coenzyme  b)  transition state…

A: An enzyme is usually made up of protein with different amino acids linked together by peptide bonds.…

Q: In lab 4, you calculated cholesterol levels of a sample directly based on the absorbance ratio of…

A: In laboratory experiments involving the quantification of cholesterol levels, precise and reliable…

Q: A researcher was studying red blood cells from a patient homozygous for the sickle cell mutation in…

A: In sickle cell anemia, a genetic condition, red blood cells can become deformed and "sickle-shaped"…

Q: The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/v) versus the…

A: The enzymes are biological catalysts that increase the rate of biochemical reactions.The enzyme…

Q: Are the given examples representative of acid-base catalysis, covalent catalysis, or metal ion…

A: Enzymes are proteinaceous entities that help the precedence of chemical reactions. The reactions…

Q: Depicted above are the Ramachandran plots for Glycine and Alanine. Why do acceptable values for…

A: Peptide conformations are restricted by the dihedral angles phi and psi. The peptide bond has a…

Q: R is the highly active form of the enzyme and T is the less active form of the enzyme. Assume that…

A: Positively cooperative enzymes demonstrate regulatory behavior in which binding a substrate molecule…

Q: An example of omega-3 fatty acid is? Arachidonic acid Alpha-linolenic acid Linoleic acid Oleic acid

A: Long chains of hydrogen-attached carbon atoms give rise to the chemical compounds known as fatty…

Q: Consider an alpha-helix comprised of twelve amino acid residues. How many hydrogen bonds should be…

A: Proteins are linear polymers of amino acids which form the basic unit. Amino acids consist of a…

Q: The diagram shows the catalytic hydrolysis of sucrose into the molecules glucose and fructose by the…

A: There are four classes of biological macromolecules: proteins, nucleic acids, lipids and…

Q: Activity of a protein as a function of pH 100 Percent activity (%) 8 50 55 60 6.5 7.0 75 80 8.5 PH

A: Chymotrypsin is a proteolytic enzyme. It acts on proteins and cleaves only specific bonds in…

Q: How many possible dipeptides can be formed from the amino acids aspartic acid, glutamine,…

A: Amino acids are biomolecules that have a hydrogen, a carboxyl group, an amino group and a chemically…

Q: beach in California and caught cute little crab and wanted to take it home. Knowing that it wouldn't…

A: Strength of a solution = mass of solute in grams / volume of solute in litresHere the solute is…

Q: The major difference between a protein molecule in its native state and in its denatured state lies…

A: The protein molecule is 150 residues long. So, there is 149 peptide bonds. It has been said that, in…

Q: The graph shows the oxygen-binding curves for myoglobin and hemoglobin. Label the graph and answer…

A: Fractional Saturation (θ) is the fraction of protein molecules saturated with ligands. (since it is…

Q: Draw an oxygen binding curve of Hb at a pH of 7.4 and another curve where all 2,3 BPG has been…

A: Hemoglobin is a heterotetrameric oxygen transport protein that is found in red blood cells or…

Q: Are the given reactions examples of general acid/base catalysis, covalent catalysis, catalysis by…

A: Enzymes catalyze reactions using various types of mechanisms. Some of the most observed mechanisms…

Q: draw a gel with samples treated similarly with components below

A: Gel electrophoresis is a separation technique of charge molecules based on their size (molecular…

Q: f) Identify -R groups that: Are hydrophobic, hydrophilic and aromatic • Are the H-bond donors and…

A: In the study of peptides and proteins, understanding their structural and chemical properties is…

Q: Draw a diagram of the hydrogen bonding interactions in: i) a two-stranded antiparallel beta sheet,…

A: Secondary structure of protein: Formed due to twisting of polypeptide chain.The folding is due to…

Q: How would the following enzymes speed up or slow down glycolysis? - high levels of Amp - high levels…

A: In glycolysis, a 6-carbon molecule of glucose-6-phosphate is broken down into 3-carbon pyruvate. It…

Q: Two possible point mutations are the substitution of lysine for leucine or the substitution of…

A: Amino acid mutations refer to changes in the DNA sequence that result in alterations to the sequence…

Q: Classify the following descriptions of enzyme inhibition as either reversible inhibition or…

A: Enzymes are high molecular weight proteins that catalyse biochemical reactions. They contain an…

Q: Which solution conditions would be best used for eluting a transcription factor from a DNA affinity…

A: We need to identify the solution conditions used for eluting a transcription factor from a DNA…

Q: Each of the reactions is catalyzed by an enzyme. For each reaction, classify the enzyme according to…

A: Most of the enzymes are divided into six major classes. They are1. Oxidoreductases2. Transferases3.…

Q: DNA sometimes has chemical groups attached, called methyl groups, that affect gene expression.…

A: Methyl groups on DNA have a significant role in epigenetics and gene regulation and have a strong…

Q: In the peptide shown below, a covalent bond that could rotate to form secondary structure is…

A: Two types of secondary structures are abundant in protein: alpha helix and beta sheets. The alpha…

Q: Decide whether each of the following statements is true about pyruvate decarboxylase. It…

A: It is an enzyme which catalyses the reaction of decarboxylation of pyruvic acid in to acetaldehyde.…

Q: Rank these three amino acids from most polar to least polar: +H₂N-CH-C-O CH-OH CH3 *H₂N-CH-C-o CH₂…

A: Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…

Q: Suppose the molecule in the drawing area below were treated with Benedict's reagent. Edit the…

A: There are four types of biological macromolecules- proteins, nucleic acids, carbohydrates and…

Q: Would the base pair Guanosine and Cytosine be more or less stable at pH 10

A: The stability of a base pair like Guanosine (G) and Cytosine (C) can be influenced by pH, but in the…

Q: After completing your analysis of the different bacterial methyltransferases at MethylTranspharmiX,…

A: Reversible enzyme inhibition can be of 4 types generally. They…

Q: The amino acid at the β82 position is in the central cavity that binds 2,3-bisphosphoglycerate in…

A: Asparagine is a neutral amino acid while lysine is positively charged amino acid. Lysine being in…

Q: The pH is O High; Low Low; High in the lungs and in the muscles. O High in the lungs but there is no…

A: A substance's pH indicates how acidic or alkaline it is. "H" stands for hydrogen, and the pH scale…

Q: o 1. Protein tyrosine phosphatase enzymes are important regula- tory enzymes. Clinical trials show…

A: Michaelis Menton equationFor a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton…

Q: Which mechanism does NOT regulate the activity of an enzyme? a competitive inhibitor binding to the…

A: Enzyme inhibition is a technique used by our body to regulate the activity of enzymes. Enzyme…

Q: Why does pyruvate either form acoa or lactate? What are the conditions

A: The conversion of pyruvate depends on oxygen availability:1) Aerobic Conditions (With Oxygen):…

Q: Match the THE BEST DESCRIPTION with the proper enzyme. RNA Polymerase I RNA Polymerase II RNA…

A: The central dogma of molecular biology is a theory that describes the flow of genetic information in…