Structural and functional analysis of SilP, a P1-type ATPase from the sil family involved in bacterial silver resistance.
Lead Research Organisation:
University of Nottingham
Department Name: Sch of Biosciences
Abstract
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People |
ORCID iD |
David Scott (Primary Supervisor) |
Studentship Projects
Project Reference | Relationship | Related To | Start | End | Student Name |
---|---|---|---|---|---|
BB/M008770/1 | 30/09/2015 | 31/03/2024 | |||
1944724 | Studentship | BB/M008770/1 | 30/09/2017 | 29/09/2021 |
Description | The results thus far contribute to the understanding of how bacterial silver resistance is carried out within bacteria. The structure of one of the proteins involved in this method has now been solved with a couple more hopefully not too far off as well. Understanding the structure of the proteins involved we can look at areas to target that will stop their activity and thus stop the bacteria being resistant to silver. |
Exploitation Route | The findings of this work can be used to find and/or design drugs that will inhibit this method of bacterial resistance and kill the bacteria. |
Sectors | Healthcare Pharmaceuticals and Medical Biotechnology |
Description | Open Day event |
Form Of Engagement Activity | Participation in an open day or visit at my research institution |
Part Of Official Scheme? | No |
Geographic Reach | Local |
Primary Audience | Schools |
Results and Impact | Several schools of students going from GCSE into A-Level attended. I gave demonstrations based on X-Ray crystallography, with crystal trays of lysozyme for the students to look at. Many of the students asked questions as to the reason behind crystallography, these were answered with regards to drug development and biological mechanisms within the body. |
Year(s) Of Engagement Activity | 2018,2020 |