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Condensation reactions likely played major roles in the synthesis of the first biotic molecules including early peptides and nucleic acids.In fact, condensation reactions would be required at multiple steps in RNA oligomerization: the condensation of nucleobases and sugars, nucleoside phosphorylation, and nucleotide polymerization.
Condensation of long double-helical DNAs is a sharp phase transition, which takes place within a narrow interval of condensing agent concentrations.[ref] Since the double helices come very closely to each other in the condensed phase, this leads to the restructuring of water molecules, which gives rise to the so-called hydration forces.[ref] To ...
In biology the term 'condensation' is used much more broadly and can also refer to liquid–liquid phase separation to form colloidal emulsions or liquid crystals within cells, and liquid–solid phase separation to form gels, [1] sols, or suspensions within cells as well as liquid-to-solid phase transitions such as DNA condensation during ...
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
Pages in category "Condensation reactions" The following 38 pages are in this category, out of 38 total. This list may not reflect recent changes. ...
Generic hydrolysis reaction. (The 2-way yield symbol indicates a chemical equilibrium in which hydrolysis and condensation are reversible.). Hydrolysis (/ h aɪ ˈ d r ɒ l ɪ s ɪ s /; from Ancient Greek hydro- 'water' and lysis 'to unbind') is any chemical reaction in which a molecule of water breaks one or more chemical bonds.
In molecular biology, the condensation domain is a protein domain found in many multi-domain enzymes which synthesise peptide antibiotics. This domain catalyses a condensation reaction to form peptide bonds in non-ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pp-binding).
Figure 2. Subunit composition of condensin complexes. Many eukaryotic cells possess two different types of condensin complexes, known as condensin I and condensin II, each of which is composed of five subunits (Figure 2). [4]