Abstract
The long-term goal of this project is to develop methods to predict the functional regions of proteins of unknown function. The results of previous studies have suggested that one of the largest pockets on a protein surface is most likely to be the ligand binding site. We tested if adding a measure related to local flexibility would make this prediction more accurate. We tested the hypothesis that considering the relative X-ray crystallographic B-factors (temperature factors) of atoms in a protein structure in addition to the relative sizes of surface pockets can help in identifying the functional regions of proteins.
Highlights
236-Pos Polyethylene Glycol Size and Protein-Complex Stability Francis J
We further confront these results with binding affinities calculated for ultradiluted conditions by means of free-energy perturbation (FEP) calculations
We examined the effect of polyethylene glycol (PEG) on protein-complex stability at 298 K
Summary
236-Pos Polyethylene Glycol Size and Protein-Complex Stability Francis J. Protein - ligand interactions and their good understanding are necessary for rational structure-based drug design. It is currently not possible to design a high-affinity and high-specificity small molecule compound based on the protein structure alone.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
