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- Introduction to Protein Folding and Misfolding
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1. Protein folding and misfolding: from theory to therapy
- Prof. Christopher Dobson
- Stability and Kinetics of Protein Folding
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2. Mechanisms of protein folding reactions
- Prof. Thomas Kiefhaber
- Protein Folding Theory
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3. Mapping disordered proteins with single-molecule FRET
- Dr. Hagen Hofmann
- Protein Folding Simulations
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4. Protein folding
- Prof. Eugene Shakhnovich
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5. Simulating protein folding with full atomistic detail
- Prof. Vijay Pande
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6. Molecular dynamics simulations of protein dynamics, unfolding and misfolding
- Prof. Valerie Daggett
- Protein Folding Inside the Cell: Chaperones
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7. Protein folding Inside the cell: macromolecular crowding and protein aggregation
- Prof. Emeritus R. John Ellis
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8. Chaperone mechanisms in cellular protein folding
- Prof. Dr. F. Ulrich Hartl
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9. Quality control of proteins mislocalized to the cytosol
- Dr. Ramanujan Hegde
- Protein Misfolding and Disease
- Protein Design
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11. Designing proteins with life sustaining activities 1
- Prof. Michael Hecht
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12. Designing proteins with life sustaining activities 2
- Prof. Michael Hecht
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13. Folding and design of helical repeat proteins
- Prof. Lynne Regan
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14. Design and engineering of zinc-finger domains
- Prof. Jacqui Matthews
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15. Prediction and design of protein structures and interactions
- Prof. David Baker
- Amyloid Fibrils: Structure, Formation and Nanotechnology
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16. Amyloid fibrils as functional nanomaterials
- Prof. Juliet Gerrard
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17. Functional amyloid fibrils from fungi and viruses
- Prof. Margaret Sunde
- Intrinsically disordered Proteins
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18. Fuzzy protein theory for disordered proteins
- Prof. Monika Fuxreiter
- Intersection of RNA, translation and protein aggregation.
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19. Expanding roles of RNA-binding proteins in neurodegenerative diseases
- Prof. Aaron D. Gitler
- Proteostasis
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20. Adapting proteostasis to ameliorate aggregation-associated amyloid diseases
- Dr. Jeffery W. Kelly
- Archived Lectures *These may not cover the latest advances in the field
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21. Amyloidosis: disease caused by amyloid
- Prof. Mark Pepys
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22. Protein folding and dynamics from single molecule spectroscopy
- Prof. Dr. Benjamin Schuler
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23. Prion diseases
- Prof. Fred Cohen
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25. Titin I27: a protein with a complex folding landscape
- Dr. Jane Clarke
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26. Novel proteins from designed combinatorial libraries
- Prof. Michael Hecht
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28. The sequence determinants of amyloid fibril formation
- Prof. Fabrizio Chiti
Printable Handouts
Navigable Slide Index
- Introduction
- Molecular interactions are critical to life
- Protein interactions
- The basis for molecular intelligence of proteins
- Artificial intelligence
- Fuzzy logic
- Fuzzy logic in everyday life
- Fuzzy logic and protein interactions
- Traditional view of proteins
- Classical structure-function paradigm
- Structural diversity - phenotypes
- Structural diversity – context dependence
- Establishing a new view
- Intrinsically disordered proteins (IDPs) (1)
- Intrinsically disordered proteins (IDPs) (2)
- Folding coupled to binding
- IDP interactions (1)
- IDP interactions (2)
- Disorder in IDP complexes
- Concept of fuzzy complexes
- Topological categories of fuzzy complexes
- Structural evidence for fuzzy complexes
- Functional evidence for fuzzy complexes
- The fuzzy concept for proteins
- Fuzziness and variation of protein functions (1)
- Fuzziness and variation of protein functions (2)
- Dynamics controls protein function
- FuzDB: fuzzy complexes database
- Molecular mechanisms of fuzzy complexes (1)
- Molecular mechanisms of fuzzy complexes (2)
- Fuzziness and context-dependence
- Evolution of cooperativity (1)
- Evolution of cooperativity (2)
- A fuzzy motif enables cooperativity
- Fuzzy regions in transcription factors
- Fuzziness and cell differentiation (1)
- Fuzziness and cell differentiation (2)
- Fuzziness and cell differentiation (3)
- Fuzziness and cell differentiation (4)
- Fuzziness and cell differentiation (5)
- Fuzziness in virus replication
- Fuzziness in viral proteins
- Dogmas need to be revisited
- Higher-order assemblies (1)
- Conversion between different material states
- Higher-order assemblies (2)
- Amyloids/prions
- Static and dynamic signalosomes
- Multivalent signalosomes
- RNP granules
- Dynamics and material states (1)
- Material states and dynamics
- Dynamics and material states (2)
- Fuzziness
- Introducing a new paradigm
- Acknowledgements
Topics Covered
- Intelligent decision-making mechanisms
- Structural disorder is maintained in protein assemblies
- Mechanisms and biological consequences of fuzziness
- Conformational diversity and context-dependence
- Fuzziness in cell differentiation and transcription factor evolution
- Material state and regulation of higher-order assemblies
Links
Series:
Categories:
Talk Citation
Fuxreiter, M. (2017, March 29). Fuzzy protein theory for disordered proteins [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 22, 2024, from https://doi.org/10.69645/WYAH3217.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Monika Fuxreiter has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
A selection of talks on Clinical Practice
Transcript
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0:00
Fuzzy Theory for Disordered Proteins
by Monika Fuxreiter,
Laboratory of Protein Dynamics,
University of Debrecen, Hungary.
Today, I'm going to discuss
the molecular basis
for the intelligent decision
making of proteins
using the framework of the fuzzy theory.
0:21
All cellular processes are determined
by a vast number of interactions
between many different
kinds of biomolecules,
proteins, nucleic acids,
and small organic substrates.
Molecular organizations
and the synergy
between a variety of interactions
control the response
to the environmental signals.
Characteristics
of the biomolecular assemblies
regulate the biological output,
and ultimately, the healthy
or pathological nature
of a biochemical process.
0:58
Protein interactions
need to be selective for their partners,
which are recognized
and also need to be specific
to the circumstances
where the interactions take place.
Here I show interactions
which are specific to different tissues.
Alternative splicing
can rewire the interaction networks
in different cell types
by alternative inclusion
of the binding elements.
Protein assemblies
must also be specific to the signals
which trigger the contacts
between the molecules.
All interactions
must be tightly regulated
by the environmental conditions
which affect the temporal
and spatial characteristics
and the functional consequences
of the assembly.