The role of partially unfolded states of proteins in biological signal transduction: Photoactive Yellow Protein and AppA

Projektinformationen

UNFOLDED PROTEINS

ID Finanzhilfevereinbarung: 501495

Startdatum 1 Mai 2004

Enddatum 30 April 2006

Finanziert unter

• Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006

Gesamtkosten € 158 326,00

EU-Beitrag € 158 326,00

Koordiniert durch

UNIVERSITEIT UTRECHT
Netherlands

Ziel

Partially unfolded and/or molten-globule like states are known to play an important role in vitro, in particular for photoreceptor-mediated signalling. It has been reported that this intrinsically unstructured state offers important advantages; however for a better understanding of this phenomena, structural information about unfolded states of proteins is crucial. The aim of this project is to increase understanding of the functional role of partially unfolded states of proteins that are involved in biological transudation. This will be achieved by characterizing the structure and interactions of these states in the model system PYP (Photoactive Yellow Protein). This system is involved in designating pathway of a cryptozoic light receptor, which is believed to mediate negative photo taxis in certainhalophilic bacteria. The methods to be developed for characterizing these states will then be applied to theflavoprotein Appal, a recently discovered photoreceptor protein from Rib. Sphaeroides. The main experimental technique that will be employed is high-resolution NMR spectroscopy, in combination with computational tools, based on the Molecular Dynamics approach. They will be developed to describe the ensemble of conformers that constitute a (partially) molten globule state of a protein. These tools will have important implications for the more general questions surrounding (functional) protein folding and unfolding. Folding is thought to be involved in human pathologies such as Alzheimer disease and Creutzfeldt-Jakobdisease. Since the interaction partners are known for the Appal photoreceptor protein, this for the first time allows the complete reconstitution of the in vivo signal transudation chain, initiated by Appal.

Wissenschaftliches Gebiet

• medical and health sciences › basic medicine › neurology › dementia › alzheimer
• natural sciences › biological sciences › microbiology › bacteriology
• natural sciences › physical sciences › optics › spectroscopy › absorption spectroscopy
• natural sciences › biological sciences › biochemistry › biomolecules › proteins › protein folding
• medical and health sciences › basic medicine › pathology

Schlüsselbegriffe

• AppA
• NMR spectroscopy
• PYP
• Photoactive Yellow Protein
• computational tools
• flavoprotein
• molecular modeling
• photoreceptors
• protein folding
• transient intermediates

Programm/Programme

• FP6-MOBILITY - Human resources and Mobility in the specific programme for research, technological development and demonstration "Structuring the European Research Area" under the Sixth Framework Programme 2002-2006

Thema/Themen

• MOBILITY-2.1 - Marie Curie Intra-European Fellowships (EIF)

Aufforderung zur Vorschlagseinreichung

FP6-2002-MOBILITY-5
Andere Projekte für diesen Aufruf anzeigen

Finanzierungsplan

EIF - Marie Curie actions-Intra-European Fellowships

Koordinator

UNIVERSITEIT UTRECHT

• EU-Beitrag: Keine Daten
• Adresse: Heidelberglaan 8 ; UTRECHT ; Niederlande
• Gesamtkosten: Keine Daten