Calculate and compare the approximate MW of a protein with 682 amino acid residues in a single polypeptide chain and a homotrimeric protein with 227 amino acid residues in each subunit.
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Calculate and compare the approximate MW of a protein with 682 amino acid residues in a single polypeptide chain and a
homotrimeric protein with 227 amino acid residues in each subunit.
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- Consider a protein in which a negatively charged glutamic acid side chain (pKa = 4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa = 6.5). Part A Do you predict that this salt bridge will become stronger, become weaker, or be unaffected as pH increases from pH = 7.2 to pH = 7.8? The salt bridge will become stronger. The salt bridge will become weaker. The salt bridge will be unaffected. Submit Part B Previous Answers Correct At pH = 7.2 the glutamic acid (Glu) side chain will carry a charge of ~ -1 (at 3 pH units above the pKa for Glu, the side chain will be almost fully ionized); whereas the histidine (His) side chain will carry a charge of < +0.5 (at pH = pK₂ the charge on His would be +0.5; since pH = 7.2 is above its pKa, it will carry less (+) charge as it becomes more deprotonated). As the pH increase to 7.8, the charge on Glu will remain ~ -1 and the charge on His will decrease; thus, this salt bridge is predicted to become weaker…Provide the number of polypeptide chains present andthe number of amino acid residues in each chain. for https://www.rcsb.org/structure/6j20 Provide the molecular weight of the protein orprotein complex and the total number of atoms. (All of this information can be found in the PDBpage.) Create a figure (available in the PDB page) that shows the topology of your protein, i.e.the secondary structures adopted by different regions of the protein (alpha helix, beta strand).Make sure to also provide a figure legend that helps interpret the figure and appropriate figurecaption that briefly explains the figure.Peptides and small proteins fold spontaneously in aqueous solution at room temperature. Thus, for a small protein in water, we can say ΔG FOLD < 0. Denoting the unfolded protein as Unf and the folded protein as Fld, we can write the following equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering the transition from the unfolded state (in which there are many possible conformations) to the folded state (only one conformation), there is clearly a decrease in the entropy of the protein. However, protein folding is (correctly) described as an entropically driven process.a) Resolve this apparent paradox by identifying the enthalpy (ΔH) and entropy (−TΔS)components involved in protein…
- Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2)(pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5)(pKa=6.5).The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations available. To a first ap- proximation, the native, folded state can be thought to have one conforma- tion. The unfolded state can be estimated to have three possible orientations about cach bond between residues. (a) For a protein of 100 residues, estimate the entropy change per mole upon denaturation. (b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C? (c) Will the fraction denatured increase or decrease with increasing temperature?What would you predict about the ratio of hydrophilic to hydro- phobic amino acid residues in a series of monomeric globular proteins that range in size from a molecular weight of 10,000 g/mole to a molecular weight of 100,000 g/mole? Note that the volume of a sphere is 4/3nr³, while the sur- face area of the outside of a sphere is 4пr².
- Calculate the approximate molecular weight of a protein composed of 587 amino acid residues in a single polypeptide chain. approximate weight: in kDaThe major difference between a protein molecule in its native state and inits denatured state lies in the number of conformations available. To a firstapproximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues.(a) For a protein of 100 residues, estimate the entropy change per moleupon denaturation.(b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?(c) Will the fraction denatured increase or decrease with increasingtemperature?The major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations avail- able. To a first approximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues. (a) For a protein of 100 residues, estimate the entropy change per mole upon denaturation. (b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C? (c) Will the fraction denatured increase or decrease with increasing temperature?
- In the molecule of oligomeric protein there are 19 lysine residues. 12 of them may be easily acetylated with anhydrides of dicarbon acids (it react with NH2-groups). The acetylation of extra two residues of lysine will dissociate the protein to the subunits. The rest 5 lysine residues may be modified only after denaturation of the protein. Suggest, how many lysine residues are: a) on a surface of protein globule; b) inside globule: c) in a site which is responsible for the contact within subunitsConsider a protein in which a negatively charged glutamic acid side chain (pKa = 4.2) makes a salt bridge (ion–ion interaction) with a positively charged histidine side chain (pKa = 6.5). (a) Do you predict that this salt bridge will become stronger, become weaker, or be unaffected as pH increases from pH = 7.0 to pH = 7.5? (b) Justify your answer with calculations of partial charges on these amino acid side chains.Consider a protein in which a negatively charged glutamic acid side chain(pKa = 4.2) makes a salt bridge (ion–ion interaction) with a positively charged histidine side chain (pKa = 6.5).(a) Do you predict that this salt bridge will become stronger, become weaker, or be unaffected as pH increases from pH = 7.0 to pH = 7.5?(b) Justify your answer with calculations of partial charges on these aminoacid side chains.
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