| http://purl.uniprot.org/citations/32543177 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32543177 | http://www.w3.org/2000/01/rdf-schema#comment | "With the increasing incidence of neurodegenerative disorders, there is an urgent need to understand the protein folding process. Examining the folding process of multidomain proteins remains a prime challenge, as their complex conformational dynamics make them highly susceptible to misfolding and/or aggregation. The presence of multiple domains in a protein can lead to interaction between the partially folded domains, thereby driving misfolding and/or aggregation. Calnuc is one such multidomain protein for which Ca2+ binding plays a pivotal role in governing its structural dynamics and stability and, presumably, in directing its interactions with other proteins. We demonstrate differential structural dynamics between the Ca2+-free and Ca2+-bound forms of calnuc. In the absence of Ca2+, full-length calnuc displays equilibrium structural transitions with four intermediate states, reporting a sum of the behavioral properties of its individual domains. Fragment-based studies illustrate the sequential events of structure adoption proceeding in the following order: EF domain followed by the NT and LZ domains in the apo state. On the other hand, Ca2+ binding increases domain cooperativity and enables the protein to fold as a single unit. Single-tryptophan mutant proteins, designed in a domain-dependent manner, confirm an increase in the number of interdomain interactions in the Ca2+-bound form as compared to the Ca2+-free state of the protein, thereby providing insight into its folding process. The attenuated domain crosstalk in apo-calnuc is likely to influence and regulate its physiologically important intermolecular interactions."xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.biochem.0c00207"xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/author | "Aradhyam G.K."xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/author | "Vignesh R."xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/pages | "2507-2517"xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/title | "A Change in Domain Cooperativity Drives the Function of Calnuc."xsd:string |
| http://purl.uniprot.org/citations/32543177 | http://purl.uniprot.org/core/volume | "59"xsd:string |
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