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Printable Handouts
Navigable Slide Index
- Introduction
- Outline of talk
- Introducing the protein intrinsic disorder concept
- Classical protein structure-function paradigm
- Protein structure-function paradigm: the big bang
- Recognition of intrinsic disorder by example
- Apo-form of human alpha-fetoprotein
- Prothymosin alpha: funny protein
- Prothymosin alpha: nothing to look at
- Role of bioinformatics
- Intrinsically disordered proteins: brief history (1)
- Intrinsically disordered proteins: brief history (2)
- Intrinsically disordered proteins: brief history (3)
- New concept in protein science
- Fate of a polypeptide chain
- Protein non-folding problem
- Different depth of disorder in a whole protein
- Different levels of disorder in a protein molecule
- Protein sequence and intrinsic disorder
- Protein non-folding: why?
- Amino acid determinants of protein foldability
- Prediction of protein disorder status
- Databases for prediction
- Natural abundance of intrinsic disorder
- Abundance of intrinsically disordered proteins
- Why are IDPs abundant in different proteomes?
- Protein disorder and function
- Elucidating functional repertoire of IDPs
- Functional anthology of disordered proteins (1)
- Functional anthology of disordered proteins (2)
- Protein structure/function relationships
- Intrinsic disorder in PPI networks
- Flexible nets
- Can hub proteins and their partners be rigid?
- Intrinsic disorder and PPI networks
- HMGA1 interactome
- 14-3-3 many-to-one binding scenario
- p53 one-to-many binding scenario
- Binding plasticity (chameleon behavior)
- Naive explanation for the chameleon behavior
- Intrinsic disorder commonness in PPIs networks
- Induced folding
- MoRF types
- Small-scale movements in MoRF partner
- Large-scale movements in MoRF partner
- Perturbations in MoRF partner: partial folding
- Perturbations in MoRF partner: partial unfolding
- Static complexes vs. dynamic complexes
- IDPs play staccato: “polyelectrostatic” model
- Interaction modes attainable by IDPs
- IDP interaction modes (1)
- IDP interaction modes (2)
- Intrinsic disorder and alternative splicing
- Alternative splicing (AS)
- Abundance of disorder in AS regions
- Functional regulation via AS
- Intrinsic disorder & post-translational modifications
- Phosphorylation and protein intrinsic disorder
- PKI alpha–cAMP-D PK complex
- PTM and protein intrinsic disorder
- Intrinsic disorder in the cell: controlled chaos
- Controlled chaos
- How nature handles IDPs binding promiscuity
- Functional misfolding of IDPs: concept
- Concluding remarks
- Acknowledgements (1)
- Acknowledgements (2)
Topics Covered
- Introducing the protein intrinsic disorder concept and intrinsically disordered proteins (IDPs)
- Structural peculiarities of IDPs
- Sequence peculiarities of IDPs
- Abundance of IDPs and their functions
- Intrinsic disorder in protein interaction networks
- Peculiarities of disorder-based binding and regulation
- Why are IDPs commonly involved in protein interactions?
Talk Citation
Uversky, V.N. (2013, August 20). The roles of intrinsic disorder in protein interaction networks [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved January 24, 2021, from https://hstalks.com/bs/2606/.Publication History
Financial Disclosures
- Prof. Vladimir N. Uversky has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
The roles of intrinsic disorder in protein interaction networks
Published on August 20, 2013
43 min