Protein plasticity driven by disorder and collapse governs the heterogeneous binding of CytR to DNA

The amplitude of thermodynamic fluctuations in biological macromolecules determines their conformational behavior, dimensions, nature of phase transitions and effectively their specificity and affinity, thus contributing to fine-tuned molecular recognition. Unique among large-scale conformational ch...

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Detalles Bibliográficos
Autores principales: Munshi, Sneha, Gopi, Soundhararajan, Subramanian, Sandhyaa, Campos, Luis A, Naganathan, Athi N
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Molecular Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5934615/
https://www.ncbi.nlm.nih.gov/pubmed/29538715
http://dx.doi.org/10.1093/nar/gky176

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5934615/
https://www.ncbi.nlm.nih.gov/pubmed/29538715
http://dx.doi.org/10.1093/nar/gky176

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