Dimensional shape of RNA forminf internal basepairs wherever its sequence allows...
The nature of RNA transcript and the fact it works under different environemntal forces in cells, that makes the transcript liable to different secondery as well as tertiary structures such as hair pins, inner loops or circular loops, as the internal complementarity plays a role here, we usually study thermodynamics of RNA sequence to give us insights about RNA folding.
Dear Dr. Al-Ouqaili
DNA is made up of molecules called nucleotides, that they are attached together to form two long strands that spiral to create a structure called a double helix. When two strands of DNA come together, they form hydrogen bonds between the nucleotides in the two chains. Bond formation releases energy and thus contributes to a net increase in entropy. An additional entropy boost comes from interactions between the nucleotides in the center of the helix; these are called base-stacking interactions. This structure gives DNA physical and chemical properties that make it very stable. This stability is important because it prevents the two DNA strands from breaking apart spontaneously and plays an important role in the way DNA is copied. mRNA, in contrast, is single-stranded, that it can fold upon itself, with the folds stabilized by short areas of complementary base pairing within the molecule, forming a three-dimensional structure.
The nature of RNA transcript and the fact it works under different environemntal forces in cells, that makes the transcript liable to different secondery as well as tertiary structures such as hair pins, inner loops or circular loops, as the internal complementarity plays a role here, we usually study thermodynamics of RNA sequence to give us insights about RNA folding.
DNA is constrained becuase of its double helical nature, thus intermolecular hydrogen bonding is favored between the two strands, as every nucleotide has a partner. RNA is single stranded, thus any hydrogen bonding is intramolecular and can assume a variety of shapes based on conformation stability to maximize mismatches or torsional constraints, which may also be impacted by associated proteins.
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