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The structure of a disulfide bond can be described by its χ ss dihedral angle between the C β −S γ −S γ −C β atoms, which is usually close to ±90°. The disulfide bond stabilizes the folded form of a protein in several ways: It holds two portions of the protein together, biasing the protein towards the folded topology.
Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It includes organizations from simple dimers to large homooligomers and complexes with defined or variable numbers of subunits. [1] In contrast to the first three levels of protein structure, not all proteins will ...
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 ...
For example, a study of SDH that used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gelfiltration experiments, and enzyme kinetics experiments could reveal an important hydrogen-bonding network that stabilizes the tetrameric quaternary structure in mammalian SDH. [5]
A protein trimer often occurs from the assembly of a protein's quaternary structure. [1] The non-covalent interactions between the hydrophobic and hydrophilic regions on the polypeptides units help to stabilize the quaternary structure. Since a protein trimer is composed of multiple polypeptide subunits, it is considered an oligomer. [2]
The P456 crystal structure provided a detailed view of how coaxial stacking stabilizes the packing of RNA helices into tertiary structures. [25] In the self-splicing group II intron from Oceanobacillus iheyensis, the IA and IB stems coaxially stack and contribute to the relative orientation of the constituent helices of a five-way junction. [6]
The primary structure of a biopolymer is the exact specification of its atomic composition and the chemical bonds connecting those atoms (including stereochemistry).For a typical unbranched, un-crosslinked biopolymer (such as a molecule of a typical intracellular protein, or of DNA or RNA), the primary structure is equivalent to specifying the sequence of its monomeric subunits, such as amino ...
Protein complexes are distinct from multidomain enzymes, in which multiple catalytic domains are found in a single polypeptide chain. [1] Protein complexes are a form of quaternary structure. Proteins in a protein complex are linked by non-covalent protein–protein interactions. These complexes are a cornerstone of many (if not most ...