b the side chains of two molecules of isoleucine O ion-ion attraction O hydrogen bonding O disulfide bridge O hydrophobic interaction

Q: Explain enzyme specificity.

A: Enzymes help in maintaining life processes. They function as a catalyst to bring efficient results.…

Q: Which of the following terms best describes an enzyme? O product O reactant O catalyst O substrate

A: Enzyme are bio catalyst that increase rate of the chemical reaction.Enzyme are specific for every…

Q: 3. An organic molecule needed to make an enzyme function correctly is called a(n) subunit cofactor…

A: enzymes are the biological catalyst that takes part in the reaction inside a living organism

Q: Please Indicate the d-electron count for the iron sulfur protein in the picture. A) 6 B) 4 C) 8…

A: According to the question, we need to determine the d-electron count for the iron sulfur protein in…

Q: What are the description of the ff? Bond specificity: Group specificity: Substrate specificity:…

A: 1.Bond specificity- Bond specificity is also called as relative specificity. Enzymes showing bond…

Q: what is the relationskip between 36 1) Enomtiomevs 2) Draslueomers 3) Identical 4) Gpimev s

A: There are the concept of stereoisomers.

Q: How many amino acids in this peptide has a sidechain that is polar? HO CH3 CH3 Gly Ser Gly Ala Gly…

A: If any polar group is present in side chain of amino acid, that side chain is polar. If there is…

Q: Marie: The cell lines produce recombinant FIX and other proteins. Which biomolecule can specifically…

A: The biomolecule that can detect the presence of FIX in a full sample of other proteins: a).…

Q: Protease enzymes are a type of protein made up of: Select one: Peptide Carbohydrates Pepsin Amino…

A: Proteins that function as biological catalysts are known as enzymes. Catalysts help to speed up…

Q: 22. Enzymes that have binding sites for modulators are specifically called O a. zymogens Ob.…

A: Interpretation: Enzymes that have binding sites for modulators are specifically called by which name…

Q: The combination of multiple proteins to perform a biological function is considered the level of…

A: Proteins are polymers of amino acids. Amino acids are building blocks of proteins. The different…

Q: With reference to enzyme action, explain what is happening in the diagram below based on the…

A: The activity of enzymes are based on pH as well as the on the reaction rate.

Q: The structure of haemoglobin: A. has an alpha-beta architecture. B. is a hetero tetramer. C. is a…

A:

Q: The "lock and key hypothesis" attempts to explain the mechanism of O sharing of electrons O…

A: Enzyme Specificity The Lock and Key Hypothesis can be depicted when the substrate fits into the…

Q: Which of the following tertiary interactions is the strongest? O the hydrophobic interaction between…

A: Hydrophobic interaction happens because of non-polar side chains and they are away from polar or…

Q: H. C. он но H (a) Which of the interactions stabilizing protein tertiary structure is (a)? O…

A: The stability of the protein is dependent upon the type of interaction involved. In hydrophobic…

Q: WHAT IS THE UNCATALYZED NEUTRAL REACTION IN WATER (need to have substrate, product, and qualitative…

A:

Q: Ferratin protein contains large amounts of iron, what function might they play? O Transport O…

A: Ferritin is ubiquitous  protein  and  plays  crucial role   and it maintian  adequate supply  of…

Q: Glutamine is a OA. basic OB. acid O c. neutral O D. racemin amino acid:

A:

Q: The active site of an enzyme has a serine residue (shown below). Which of the following describes…

A: The structure of serine amino acid is as follows:

Q: protein k

A: In this question we have to explain correct answer of the above statements that is belong to Dr.…

Q: Two cystine amino acids hold together two separate beta sheets. This is an example of side chain…

A: There are various types of interactions present in proteins-  1- hydrophobic interaction 2-…

Q: A substitution of the amino acid phenylalanine for glycine at the active site of an enzyme would…

A: Answer

Q: What are the molecules on which an enzyme acts? O glucose sugar O lipids substrates

A: Enzymes catalyze chemical reactions by lowering activation energy barriers and converting substrate…

Q: hoose the amino acid most likely to serve as a proton donor in the active site of an enzyme:…

A: ANSWERE IS :

Q: The free energy for folding (delta Gfolding) of a mutant lysozyme at 25oC is – 4.1 kJ mol-1. At…

A: For any change for example A to B. The ratio can be fine by their equilibrium constant. So…

Q: For each example, identify the protein's function in the body. Actin is the major component of thin…

A: Proteins are the long macromolecules made of amino acids. There are different type os proteins found…

Q: A type of enzyme regulation, where a product acts as an inhibitor molecule, iscalled inhibition. a.…

A: In end product inhibition, end product acts as an inhibitor molecule.

Q: The factors that denature enzyme activity are temperature, pH, salinity, alcohol and surface area.…

A: Effect of temperature: Velocity of an enzyme reaction increases with increase in temperature up to a…

Q: The structure here represents NH₂ НО. ОС OH OH a dipeptide O AMP O ADP ATP a nucleoside O 'N

A:

Q: Consider the cysteine molecule. Choose the structural formula for the anion formed in base. O HS C…

A: Amino acids are those in which carbon is attached with COOH group, amino group and R group. Amino…

Q: .) If the optimum temperature of a particular enzyme is 33°C, which of the following will likely…

A: Ans (E) Optimized temperature of the enzyme is the maximum temperature at which enzyme shows maximum…

Q: a-helix is an example of ------ * O Primary structure O Quaternary structure O Tertiary structure O…

A:

Q: What is the process that involves the breaking of intermolecular forces that hold an enzyme into the…

A: We need to determine to process which breaks apart the 3d structure of enzyme.

Q: Provide the OV1 1. R-C 2. Me-

A: Note : As per guidelines first three only allowed to solve, please post it seperately thank you…

Q: Avidin is commonly found in uncooked egg white. Consuming excessive amount of uncooked egg whites is…

A: Egg whites contain high levels of avidin, a protein that binds biotin strongly. When cooked, avidin…

Q: isoleucine and proline valine and phenylalanine glutamate and arginine glutamine and serine Hydrogen…

A:

Q: What is latest development of Oxygen binding proteins(O2BIP)

A: latest development of Oxygen binding proteins(O2BIP) Oxygen-binding proteins are arguably the most…

Q: AH = - 1.2 kcal/mol; Kp = 16 nM %3D OH 1 HO AH = - 6.0 kcal/mol; N. Kp = = 76 nM OH 2 करले HOl. AH =…

A: Binding enthalpy Or ΔH for a binding process reflects the energy change of the system when it ligand…

Q: Albumin, globulin, histones and scleroproteins belong to the class of O a. Simple proteins O b.…

A: Proteins are organic compounds made up of several amino acids that are bound together by peptide…

Q: 49. Solid raw materials in cosmetics that will gradually react with carbon dioxide in the air to…

A: 49) We can use varios raw material for cosmetics but have to choose the one which Is not harmfull.so…

Q: What is the process that involves the breaking of intermolecular forces that hold an enzyme into the…

A: Enzymes are bio-catalysts that speed up the biochemical reactions occurring in the living system.…

Q: 29.) A protein with quaternary structure described as C2B2Y2 would be a C) homodimer A) homotrimer…

A: Proteins are the long chains of amino acids. Protein has different kind of structure like primary…

Q: What interactions occur between the following? a the side chains of asparagine and threonine O…

A: Hydrogen bonding: It is type of strong dipole-dipole interaction. The hydrogen attached to an…

Q: What tertiary interaction would be expected between the following amino acids H2N-CH OH CH2 CH-CH3…

A: Applying concept of tertiary interaction in amino acid.

Q: Keactrons contmued- -et ALCI2 AICla NBS hD erRoaR za/t NCI

A: The given reaction is Friedel-craft alkylation. In the given reaction a carbocation is formed which…

Q: In designing a kinase inhibitor as a chemotherapeutic agent. tissue specificity of the inhibitor is…

A:

Q: Which protein stores O: in tissues? * collagen O ferritin O hemoglobin O myoglobin

A: Which protein stores O2 in tissue?

Q: Enzyme b. Binding: Electrostatic Forces Substrates bind to receptors and enzymes through…

A:

UV Visible Spectroscopy

Spectroscopy refers to the absorption or emission of light or other radiations by matter. When a substance or chemical absorbs light or radiation, they reach an excited state followed by de-excitation or emission of the light or radiation forming distinct spectra. UV-visible spectroscopy or  ultraviolet-visible refers to the absorption and emission in the ultraviolet and visible regions of the electromagnetic spectrum.