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Hydrogen bonding networks between subunits has been shown to be important for the stability of the tetrameric quaternary protein structure.For example, a study of SDH which used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gel filtration experiments and enzyme kinetics experiments, could reveal an important hydrogen bonding network which ...
Structure of a G-quadruplex. Left: a G-tetrad. Right: an intramolecular G4 complex. [1]: fig1 In molecular biology, G-quadruplex secondary structures (G4) are formed in nucleic acids by sequences that are rich in guanine. [2] They are helical in shape and contain guanine tetrads that can form from one, [3] two [4] or four strands. [5]
(The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic & hydrophilic interactions. Protein tertiary structure is the three-dimensional shape of a protein.
In molecular biology, a guanine tetrad (also known as a G-tetrad or G-quartet) is a structure composed of four guanine bases in a square planar array. [ 1 ] [ 2 ] They most prominently contribute to the structure of G-quadruplexes , where their hydrogen bonding stabilizes the structure.
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins.
The remaining elements found in living things are primarily metals that play a role in determining protein structure. Examples include iron, essential to hemoglobin; and magnesium, essential to chlorophyll. Some elements are essential only to certain taxonomic groups of organisms, particularly the prokaryotes.
This charge screening is often fulfilled by monovalent ions. Site-bound ions stabilize specific elements of RNA tertiary structure. Site-bound interactions can be further subdivided into two categories depending on whether water mediates the metal binding. “Outer sphere” interactions are mediated by water molecules that surround the metal ion.
However, instruments have since been developed specifically for tetrad dissection; the most advanced allow easy and semi-automated separation of tetrads. Most micromanipulators use a glass fiber needle to which the spores adhere due to the formation of a water meniscus between the agar and the needle.