3 Works

Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism - data

Nehad Noby, Husam Sabah Auhim, Samuel Winter, Harley L Worthy, Pierre J Rizkallah, Stephen A Wells & Darran Dafydd Jones
The structure was detmined of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. The conformation of the functionally important cap region is significantly different to EstN7's closest relatives, forming a bridge-like structure with reduced helical...

Association of fluorescent protein pairs and its significant impact on fluorescence and energy transfer - data

Jacob R Pope, Rachel L Johnson, W David Jamieson, Harley L Worthy, Senthilkumar Kailasam, Rochelle D Ahmed, Ismail Taban, Husam Sabah Auhim, Daniel W Watkins, Pierre J Rizjallah, Oliver K Castell & D Dafydd Jones
Data set for the above titled paper. Protein crystal structure data has been deposited seperately in the PDB under the accession code 5ni3. The data set includes the data that comprise the absorbance and fluoresence spectra and various in silico models.

Data set for paper: Positive functional synergy of structurally integrated artificial protein dimers assembled by Click chemistry

Harley L Worthy, Husam Sabah Auhim, W David Jamieson, Jacob R Pope, Aaron Wall, Robert Batchelor, Rachel L Johnson, Daniel W Watkins, Pierre Rizkallah, Oliver K Castell & D Dafydd Jones
The dataset for the spectral data (absorbance and fluoresence) presented in the paper together with the full gel images that consistute Supporting Figure 4. All structural information has been submitted to the PDB with accession code 5nhn. Steady state fluoresence was performed as described in the experimental section of the related manuscript. The datasets for absorbance has given in molar absorbance coefficient so as to standardise to a protein concentrtation of 1 M. The methods...

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