Cargando…

Towards a structural biology of the hydrophobic effect in protein folding

The hydrophobic effect is a major driving force in protein folding. A complete understanding of this effect requires the description of the conformational states of water and protein molecules at different temperatures. Towards this goal, we characterise the cold and hot denatured states of a protei...

Descripción completa

Detalles Bibliográficos
Autores principales:	Camilloni, Carlo, Bonetti, Daniela, Morrone, Angela, Giri, Rajanish, Dobson, Christopher M., Brunori, Maurizio, Gianni, Stefano, Vendruscolo, Michele
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group 2016
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4962056/ https://www.ncbi.nlm.nih.gov/pubmed/27461719 http://dx.doi.org/10.1038/srep28285

Ejemplares similares

Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein
por: Toto, Angelo, et al.
Publicado: (2016)

Inversion of the Balance between Hydrophobic and Hydrogen Bonding Interactions in Protein Folding and Aggregation
por: Fitzpatrick, Anthony W., et al.
Publicado: (2011)

Understanding the effect of alternative splicing in the folding and function of the second PDZ from Protein Tyrosine Phosphatase-BL
por: Di Silvio, Eva, et al.
Publicado: (2015)

Mapping the Protein Fold Universe Using the CamTube Force Field in Molecular Dynamics Simulations
por: Kukic, Predrag, et al.
Publicado: (2015)

A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins
por: Karlsson, Elin, et al.
Publicado: (2019)

A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation
por: Abeln, Sanne, et al.
Publicado: (2014)

Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics
por: Bonomi, Massimiliano, et al.
Publicado: (2016)

A structural ensemble of a ribosome-nascent chain complex during co-translational protein folding
por: Cabrita, Lisa D., et al.
Publicado: (2016)

In-Cell NMR Characterization of the Secondary Structure Populations of a Disordered Conformation of α-Synuclein within E. coli Cells
por: Waudby, Christopher A., et al.
Publicado: (2013)

Transactivation domain of Adenovirus Early Region 1A (E1A): Investigating folding dynamics and aggregation
por: Sharma, Nitin, et al.
Publicado: (2022)

Metainference: A Bayesian inference method for heterogeneous systems
por: Bonomi, Massimiliano, et al.
Publicado: (2016)

An Outlook on the Complexity of Protein Morphogenesis in Health and Disease
por: Brunori, Maurizio, et al.
Publicado: (2022)

Cotranslational Protein Folding and Terminus Hydrophobicity
por: Srivastava, Sheenal, et al.
Publicado: (2011)

Hidden kinetic traps in multidomain folding highlight the presence of a misfolded but functionally competent intermediate
por: Gautier, Candice, et al.
Publicado: (2020)

A Small Molecule Stabilizes the Disordered Native State of the Alzheimer’s Aβ Peptide
por: Löhr, Thomas, et al.
Publicado: (2022)

Tolerance of Protein Folding to a Circular Permutation in a PDZ Domain
por: Hultqvist, Greta, et al.
Publicado: (2012)

Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs
por: Papaleo, Elena, et al.
Publicado: (2018)

Towards hydrophobic carminic acid derivatives and their incorporation in polyacrylates
por: Gabrielli, Luca, et al.
Publicado: (2018)

Unveiling the folding mechanism of the Bromodomains
por: Petrosino, Maria, et al.
Publicado: (2017)

The H50Q Mutation Induces a 10-fold Decrease in the Solubility of α-Synuclein
por: Porcari, Riccardo, et al.
Publicado: (2015)

The Structure of a Conserved Domain of TamB Reveals a Hydrophobic β Taco Fold
por: Josts, Inokentijs, et al.
Publicado: (2017)

Modularity of the hydrophobic core and evolution of functional diversity in fold A glycosyltransferases
por: Venkat, Aarya, et al.
Publicado: (2022)

Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases
por: Gadhave, Kundlik, et al.
Publicado: (2020)

The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments
por: Granata, Daniele, et al.
Publicado: (2015)

Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability
por: Camilloni, Carlo, et al.
Publicado: (2016)

Desolvation and Development of Specific Hydrophobic Core Packing during Im7 Folding
por: Bartlett, Alice I., et al.
Publicado: (2010)

Native Contact Density and Nonnative Hydrophobic Effects in the Folding of Bacterial Immunity Proteins
por: Chen, Tao, et al.
Publicado: (2015)

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules
por: Falcon, Benjamin, et al.
Publicado: (2019)

Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms
por: Kukic, Predrag, et al.
Publicado: (2015)

Structural biology of the PCI-protein fold
por: Ellisdon, Andrew M., et al.
Publicado: (2012)

AlphaFold and the future of structural biology
por: Read, Randy J., et al.
Publicado: (2023)

The Mechanism of Folding of Im7 Reveals Competition between Functional and Kinetic Evolutionary Constraints
por: Friel, Claire T., et al.
Publicado: (2009)

A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation
por: Kundra, Rishika, et al.
Publicado: (2020)

The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands
por: Radauer, Christian, et al.
Publicado: (2008)

Therapeutic Interventions of Cancers Using Intrinsically Disordered Proteins as Drug Targets: c-Myc as Model System
por: Kumar, Deepak, et al.
Publicado: (2017)

Targeting the nsp2 Cysteine Protease of Chikungunya Virus Using FDA Approved Library and Selected Cysteine Protease Inhibitors
por: Kumar, Prateek, et al.
Publicado: (2019)

Mitoxantrone dihydrochloride, an FDA approved drug, binds with SARS-CoV-2 NSP1 C-terminal
por: Kumar, Prateek, et al.
Publicado: (2022)

FuzDrop on AlphaFold: visualizing the sequence-dependent propensity of liquid–liquid phase separation and aggregation of proteins
por: Hatos, Andras, et al.
Publicado: (2022)

Nature and Regulation of Protein Folding on the Ribosome
por: Waudby, Christopher A., et al.
Publicado: (2019)

Emergence and evolution of an interaction between intrinsically disordered proteins
por: Hultqvist, Greta, et al.
Publicado: (2017)

Cannot write session to /tmp/vufind_sessions/sess_nq7hme0pf1sj1htotaa8q90ir1