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- W1970054503 abstract "Multi-domain proteins have many advantages with respect to stability and folding inside cells. Here we attempt to understand the intricate relationship between the domain-domain interactions and the stability of domains in isolation. We provide quantitative treatment and proof for prevailing intuitive ideas on the strategies employed by nature to stabilize otherwise unstable domains. We find that domains incapable of independent stability are stabilized by favourable interactions with tethered domains in the multi-domain context. Stability of such folds to exist independently is optimized by evolution. Specific residue mutations in the sites equivalent to inter-domain interface enhance the overall solvation, thereby stabilizing these domain folds independently. A few naturally occurring variants at these sites alter communication between domains and affect stability leading to disease manifestation. Our analysis provides safe guidelines for mutagenesis which have attractive applications in obtaining stable fragments and domain constructs essential for structural studies by crystallography and NMR." @default.
- W1970054503 created "2016-06-24" @default.
- W1970054503 creator A5062925169 @default.
- W1970054503 creator A5076920718 @default.
- W1970054503 date "2011-07-18" @default.
- W1970054503 modified "2023-10-18" @default.
- W1970054503 title "Stability of domain structures in multi-domain proteins" @default.
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- W1970054503 doi "https://doi.org/10.1038/srep00040" @default.
- W1970054503 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3216527" @default.
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