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1. Introduction
2. Outline of talk
3. Introducing the protein intrinsic disorder concept
4. Classical protein structure-function paradigm
5. Protein structure-function paradigm: the big bang
6. Recognition of intrinsic disorder by example
7. Apo-form of human alpha-fetoprotein
8. Prothymosin alpha: funny protein
9. Prothymosin alpha: nothing to look at
10. Role of bioinformatics
11. Intrinsically disordered proteins: brief history (1)
12. Intrinsically disordered proteins: brief history (2)
13. Intrinsically disordered proteins: brief history (3)
14. New concept in protein science
15. Fate of a polypeptide chain
16. Protein non-folding problem
17. Different depth of disorder in a whole protein
18. Different levels of disorder in a protein molecule
19. Protein sequence and intrinsic disorder
20. Protein non-folding: why?
21. Amino acid determinants of protein foldability
22. Prediction of protein disorder status
23. Databases for prediction
24. Natural abundance of intrinsic disorder
25. Abundance of intrinsically disordered proteins
26. Why are IDPs abundant in different proteomes?
27. Protein disorder and function
28. Elucidating functional repertoire of IDPs
29. Functional anthology of disordered proteins (1)
30. Functional anthology of disordered proteins (2)
31. Protein structure/function relationships
32. Intrinsic disorder in PPI networks
33. Flexible nets
34. Can hub proteins and their partners be rigid?
35. Intrinsic disorder and PPI networks
36. HMGA1 interactome
37. 14-3-3 many-to-one binding scenario
38. p53 one-to-many binding scenario
39. Binding plasticity (chameleon behavior)
40. Naive explanation for the chameleon behavior
41. Intrinsic disorder commonness in PPIs networks
42. Induced folding
43. MoRF types
44. Small-scale movements in MoRF partner
45. Large-scale movements in MoRF partner
46. Perturbations in MoRF partner: partial folding
47. Perturbations in MoRF partner: partial unfolding
48. Static complexes vs. dynamic complexes
49. IDPs play staccato: “polyelectrostatic” model
50. Interaction modes attainable by IDPs
51. IDP interaction modes (1)
52. IDP interaction modes (2)
53. Intrinsic disorder and alternative splicing
54. Alternative splicing (AS)
55. Abundance of disorder in AS regions
56. Functional regulation via AS
57. Intrinsic disorder & post-translational modifications
58. Phosphorylation and protein intrinsic disorder
59. PKI alpha–cAMP-D PK complex
60. PTM and protein intrinsic disorder
61. Intrinsic disorder in the cell: controlled chaos
62. Controlled chaos
63. How nature handles IDPs binding promiscuity
64. Functional misfolding of IDPs: concept
65. Concluding remarks
66. Acknowledgements (1)
67. 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?

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

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 February 21, 2020, from https://hstalks.com/bs/2606/.

Publication History

• Published on August 20, 2013

Financial Disclosures

• Prof. Vladimir N. Uversky has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.