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These findings will further our understanding of the factors involved in stabilizing protein structure.
Disulfide bonds play an important role in stabilizing protein structure and regulating protein function.
Water molecules can have important roles in stabilizing protein structure and therefore where possible, buried water molecules that form stabilizing interactions in template structures should be incorporated into homology models before minimization.
Complex salt bridges have been investigated for their role in stabilizing protein structure and protein-protein interactions [ 52, 56– 60].
The first class of PTMs is crucial for providing moieties for catalytic functions, for modifying enzyme activities or for stabilizing protein structure.
Although particular motifs have previously been identified where buried polar residues have conserved roles in stabilizing protein structure, for example in helix capping, we demonstrate that such interactions occur in a range of architectures and highlight those polar amino acid types that fulfil these roles.
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Many gene families, especially those for stabilizing protein structures and removing toxic substances from cells, are highly expanded in B. platifrons, indicating adaptation to extreme environmental conditions.
The different roles played by conventional non-covalent and cation π interactions in stabilizing protein structures have been investigated using a dataset of 62 non-redundant DNA binding proteins.
Zn2+ plays a crucial role in stabilizing protein structures (Hanson [2008]).
In addition to HSPs, trehalose is also involved in stabilizing protein structures in order to prevent protein denaturation and aggregation (Singer and Lindquist 1998).
No increases were seen in GFP accumulation, suggesting that selenocystamine plays a role in stabilizing protein structures through the formation of disulfide bonds and potentially mitigating degradation of un-folded polypeptides.
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