Research Project:
Computational redesign to change conformation and activity of a redox protein.

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crispj.investigatorPandey, Amit Vikram
crispj.investigator.affiliationClinic of Paediatric Medicine
dc.date.accessioned2025-06-17T06:42:13Z
dc.date.available2025-06-17T06:42:13Z
dc.description.abstractBackground: NADPH cytochrome P450 oxidoreductase (POR) is very important for metabolic processes in all mammals. Previously we have shown that mutations in this protein can cause serious health problems. While we know that POR supports other proteins to do their jobs, we don't fully understand how changes in POR affect its work with these other proteins. Rationale: POR has a complicated structure that helps it work with over 50 different proteins. One of its main partners is a group of proteins called cytochrome P450s, which help with many chemical reactions in living things. We want to create new versions of POR that can be used in different applications. By studying these new versions, we hope to learn more about how POR works and how we can control its activity. Experiments and Aims: 1. Designing New POR Proteins: In Switzerland, we'll use computer programs to design many new versions of POR. We'll test these new versions in human cells and bacteria to see how well they work with cytochrome P450s. 2. Mechanism Studies: With our collaborators, we'll look at POR molecules to see how they move, change shape and interact with partner proteins. This will help us understand how POR works on a very detailed level. Significance: By understanding how POR works and creating new versions of it, we can improve its use in various applications, like cleaning up oil spills or making new medicines. This research will help us understand the basic principles of how proteins work and how we can design them for specific tasks.
dc.description.sponsorshipClinic of Paediatric Medicine
dc.description.sponsorshipUniversity of Bern, Human Medicine
dc.identifier.urihttps://boris-portal.unibe.ch/handle/20.500.12422/211333
dc.language.isoen
dc.relation.funding229294
dc.subject.ddc500 - Science::570 - Life sciences; biology
dc.subject.ddc600 - Technology::610 - Medicine & health
dc.subject.keywordsprotein folding
dc.subject.keywordstailored enzymes
dc.subject.keywordsprotein conformation
dc.subject.keywordsComputational redesign
dc.subject.keywordsprotein engineering
dc.subject.keywordsRedox biology
dc.subject.keywordsprotein stability
dc.subject.keywordsCytochrome P450
dc.subject.keywordsP450 oxidoreductase
dc.subject.keywordsDesigner proteins
dc.subject.keywordsSynthetic biology
dc.subject.keywordsMachine Learning
dc.subject.keywordsProtein design
dc.subject.keywordsProtein modelling
dc.subject.keywordsComputational structural biology
dc.titleComputational redesign to change conformation and activity of a redox protein.
dspace.entity.typeProject
local.fakeitemtrue
local.submitter
oairecerif.amount397559
oairecerif.amount.currencyCHF
oairecerif.funderSwiss National Science Foundation
oairecerif.funding.endDate2029-03-31
oairecerif.funding.startDate2025-04-01
oairecerif.fundingParentSNF
oairecerif.identifier.urlhttps://data.snf.ch/grants/grant/229294
oairecerif.project.startDate2025-04-01
unibe.funding.accesstypePublic
unibe.funding.creditholderPandey, Amit Vikram
unibe.funding.fundertypePublic
unibe.funding.typePublic Grant
unibe.primaryconductorUniversity of Bern, Human Medicine
unibe.primarycontact.affiliationClinic of Paediatric Medicine
unibe.project.expectedcompletionDate2029-03-31
unibe.project.primarycontactPandey, Amit Vikram

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