Title : Importance of protein intrinsic conformational dynamics and transient nature of non-covalent interactions in ligand binding affinity.

Pub. Date : 2021 Dec 1

PMID : 34655583






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 BEN1 contains an NADP+ binding domain and possesses acidic N-terminal extension essential for interaction with A. thaliana SerRS. NADP NAD(P)-binding Rossmann-fold superfamily protein Arabidopsis thaliana
2 By performing microscale thermophoresis (MST) experiments we have shown that both BEN1 variants bind the NADP+ cofactor, however, truncated BEN1 showed 34-fold higher affinity towards NADP+ indicating that its core protein structure is not just preserved but it binds NADP+ even stronger. NADP NAD(P)-binding Rossmann-fold superfamily protein Arabidopsis thaliana
3 By performing microscale thermophoresis (MST) experiments we have shown that both BEN1 variants bind the NADP+ cofactor, however, truncated BEN1 showed 34-fold higher affinity towards NADP+ indicating that its core protein structure is not just preserved but it binds NADP+ even stronger. NADP NAD(P)-binding Rossmann-fold superfamily protein Arabidopsis thaliana
4 By performing microscale thermophoresis (MST) experiments we have shown that both BEN1 variants bind the NADP+ cofactor, however, truncated BEN1 showed 34-fold higher affinity towards NADP+ indicating that its core protein structure is not just preserved but it binds NADP+ even stronger. NADP NAD(P)-binding Rossmann-fold superfamily protein Arabidopsis thaliana
5 Our results have shown that both truncated and intact BEN1 variants form the same number of interactions with the NADP+ cofactor; however, it was the interaction occupancy that was affected. NADP NAD(P)-binding Rossmann-fold superfamily protein Arabidopsis thaliana