Grant: Operating Grant
University of Toronto
$774,730.00
Biophysical principles of intra- and inter-molecular recognition in protein folding and interactions involving disordered proteins
FY 2011-12
Summary
Advances in modern biomedical research depend on a knowledge of the molecular basis of life. Proteins are a diverse class of biomolecules performing various vital functions in all living things. The three dimensional shape --- or shapes --- of a protein is encoded by its specific sequence of amino acids, and this sequence is in turn encoded by a gene. For some proteins, folding into a highly ordered globular shape is essential for function, whereas misfolding can lead to diseases such as Alzheimer's and Parkinson's. In this context, switch-like folding is important for avoiding undesirable, disease-causing aggregation. For other proteins, however, a disordered form is necessary for them to function. Therefore, developing a fundamental understanding of how proteins fold and unfold is of great intellectual and technological significance, and will benefit all areas of biomedical research. Ultimately, this knowledge should be deducible from chemistry and physics. Currently, however, it is not yet feasible in most cases to predict a protein's folding and dynamic behaviours from its amino acid sequence because no one understands well enough the intricate forces that guide some proteins to fold while the same set of basic forces can lead other proteins to adopt a fuzzy collection of disordered shapes. Current knowledge is also limited as to the forces that lead proteins to recognize their specific partners, a process that is crucial for biological function. Taking clues from available data and working closely with experimentalists, we will develop computational models toward systematically unraveling the workings of these forces.
Department
Program
Operating Grant
Recipient
Location
Ontario, Canada
Recipient Type
Academia
Type
Grant
Source
CIHR Funding Decisions Database
As published
Id
252624
Name
Chan Hue Sun
Region
Ontario
Country
Canada
Orgtype
Institution Paid; Research Institution
Instname2
Genetics
Theme2
Biomedical
Prcname2
Biochemistry & Molecular Biology - A
Projecttitle
Biophysical principles of intra- and inter-molecular recognition in protein folding and interactions involving disordered proteins
Programtype2
Operating Grants
Orgnameinp2
University of Toronto
Cihramount2
$774,730
Cihrequipment2
$0
Programname2
Operating Grant
Keyworddelim
Biophysics Of Solvation And Its Role In Protein Behaviour; Computational Modeling; Cooperativity And Intrinsic Disorder; Many-Body Interactions; Protein Dynamics; Protein Folding And Protein-Protein Interactions
Abstract
Advances in modern biomedical research depend on a knowledge of the molecular basis of life. Proteins are a diverse class of biomolecules performing various vital functions in all living things. The three dimensional shape --- or shapes --- of a protein is encoded by its specific sequence of amino acids, and this sequence is in turn encoded by a gene. For some proteins, folding into a highly ordered globular shape is essential for function, whereas misfolding can lead to diseases such as Alzheimer's and Parkinson's. In this context, switch-like folding is important for avoiding undesirable, disease-causing aggregation. For other proteins, however, a disordered form is necessary for them to function. Therefore, developing a fundamental understanding of how proteins fold and unfold is of great intellectual and technological significance, and will benefit all areas of biomedical research. Ultimately, this knowledge should be deducible from chemistry and physics. Currently, however, it is not yet feasible in most cases to predict a protein's folding and dynamic behaviours from its amino acid sequence because no one understands well enough the intricate forces that guide some proteins to fold while the same set of basic forces can lead other proteins to adopt a fuzzy collection of disordered shapes. Current knowledge is also limited as to the forces that lead proteins to recognize their specific partners, a process that is crucial for biological function. Taking clues from available data and working closely with experimentalists, we will develop computational models toward systematically unraveling the workings of these forces.
Competitiondate
201203
Approvedterm2
5 yrs 0 mth
Pinamesdelim
Chan, Hue Sun
Approvedterm
5 ans 0 mois
Cihrcontribution2
~ $774,730~ $0~