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Molecular Biology- Assignment
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Added on 2020-05-16
Molecular Biology- Assignment
Added on 2020-05-16
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UNIVERSITY:NAME :STUDENT ID:COURSE CODE COURSE NAMEMolecular Biology
Molecular Biology2HOME WORK 2Question 1The double stranding of DNA can be made to be reversible and denatured at various melting points. The transition from double stranded formation helix to single strand helix, changes the absorbance of the bases at λ=260 which is associated with the transition phase. Absorbance at A260, can increase when the DNA melts reaching hyper chromatic effect. The thermal melting point of any DNA has shown that as the temperature is increased, the solution of double strand bonds denatures, leading to formation of single strand structures. The temperature level which the DNA melts is referred to as TM. The melting levels is often detected by the absorbance of 260 nm, while the coefficient of extinction in thedouble strand DNA is lowered to approximately 30% which is lower than the single strand DNA. Lowered absorption at 260 nm in the double strand DNA is often occasioned by the interactions of the dipoles present on the stacked bases, which is interrupted by the DNA single stranding.Responsible forces which influence this effect include:Hydrogen bonds-Have strong stability on the double strand DNA stability. However as the TM of the double strand increases the GC content also rises. This leads to effect on the differences on the stacking interactions and the presence of hydrogen bonds on the GC players which play a role affecting the melting of DNA.Electrostatic forces-The charged repulsion of the phosphate compounds in the DNA leads to destabilization of the bases, and it has been seen as much stronger than the non polar chains present in proteins. The bases which shows strong attachment with GC pair and the AT bases have shown to increase in TM as the content of GC increasesVan der Waals forces-They have a significant stability on the double strands of DNA. They are characterised by strong dipole interactions amongst the bases and stronger on the non polar chains of protein. The bases which are stronger stacking with GC base pairs and AT base pairs have shown increase the overall TM as the GC content increases.Question 2The stability of proteins has been found to be associated with direct associations between atoms on its backbone chain. Also increase on hydrophobic on the amino side chain are exposed. Hydrophobic does not really signify any formal interactions but rather the ability
Molecular Biology3of no polar residues to affect the overall structure of the and the fluctuation of aqueous solvent.The observable manifestation is the increase in the heat produced on the overall system,ΔCp, which results in strong temperature remittance on the transition process of enthalpy and entropy. Smalls deviations from the temperature results in thermal contribution which results in ΔH and TΔS neutralizing each other, when summed they give free energy ΔG.. But with bigger temperature range, the different functional groups of the enthalpy and entropy files high contribution of heat on the transition seen I the free energy expulsion. At times it has been observed to dominate the stability of the proteins and the ability to lead to cold denaturization process. Question 3Structure of glutamateStructure of Arginine Methyl groupHydrogen bond Hydrogen Acceptor Hydrogen Acceptor Hydrogen acceptorMethyl group Methyl group Hydrogen Donor
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