Results 71 to 80 of about 448,472 (368)

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins

International Journal of Molecular Sciences, 2020
The abundance of intrinsic disorder in the protein realm and its role in a variety of physiological and pathological cellular events have strengthened the interest of the scientific community in understanding the structural and dynamical properties of ...
G. Bianchi, S. Longhi, R. Grandori, S. Brocca   +3 more
semanticscholar   +1 more source

Intrinsic Structural Disorder in Cytoskeletal Proteins [PDF]

Cytoskeleton, 2013
Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and microtubules.
Simone Kosol, Sara Contreras Martos, Mainak Guharoy, Beáta Szabó, Peter Tompa, Peter Tompa   +5 more
openaire   +4 more sources

Self‐recognition by an intrinsically disordered protein [PDF]

FEBS Letters, 2008
The intrinsically disordered translocation domain (T‐domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T‐domain of colicin N known to bind to the helper protein TolA in target cells also ...
Hecht O, Ridley H, Boetzel R, Lewin A, Cull N, Chalton DA, Lakey JH, Moore GR   +7 more
openaire   +4 more sources

Intrinsic Disorder in Tetratricopeptide Repeat Proteins [PDF]

International Journal of Molecular Sciences, 2020
Among the realm of repeat containing proteins that commonly serve as “scaffolds” promoting protein-protein interactions, there is a family of proteins containing between 2 and 20 tetratricopeptide repeats (TPRs), which are functional motifs consisting of 34 amino acids.
Roy Khalife, Nathan W. Van Bibber, Vladimir N. Uversky, Vladimir N. Uversky, Bin Xue, Cornelia Haerle   +5 more
openaire   +4 more sources

A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon’s Information Theory

Entropy, 2019
We propose a framework to convert the protein intrinsic disorder content to structural entropy (H) using Shannon’s information theory (IT). The structural capacity (C), which is the sum of H and structural information (I), is equal to the amino acid ...
Hao-Bo Guo, Yue Ma, Gerald A. Tuskan, Hong Qin, Xiaohan Yang, Hong Guo   +5 more
doaj   +1 more source

Evolution of Intrinsic Disorder in Protein Loops

Life, 2023
Intrinsic disorder accounts for the flexibility of protein loops, molecular building blocks that are largely responsible for the processes and molecular functions of the living world. While loops likely represent early structural forms that served as intermediates in the emergence of protein structural domains, their origin and evolution remain poorly ...
Fizza Mughal, Gustavo Caetano-Anollés
openaire   +3 more sources

Making tau amyloid models in vitro: a crucial and underestimated challenge

FEBS Letters, EarlyView.
This review highlights the challenges of producing in vitro amyloid assemblies of the tau protein. We review how accurately the existing protocols mimic tau deposits found in the brain of patients affected with tauopathies. We discuss the important properties that should be considered when forming amyloids and the benchmarks that should be used to ...
Julien Broc, Clara Piersson, Yann Fichou
wiley   +1 more source

Full structural ensembles of intrinsically disordered proteins from unbiased molecular dynamics simulations

bioRxiv, 2020
Molecular dynamics (MD) simulation is widely used to complement ensemble-averaged experiments of intrinsically disordered proteins (IDPs). However, MD often suffers from limitations of inaccuracy.
Utsab R. Shrestha, Jeremy C. Smith, Loukas Petridis   +2 more
semanticscholar   +1 more source

Identification of novel small molecule inhibitors of ETS transcription factors

FEBS Letters, EarlyView.
ETS transcription factors play an essential role in tumourigenesis and are indispensable for sprouting angiogenesis, a hallmark of cancer, which fuels tumour expansion and dissemination. Thus, targeting ETS transcription factor function could represent an effective, multifaceted strategy to block tumour growth. The evolutionarily conserved E‐Twenty‐Six
Shaima Abdalla, Zary Forghany, Jin Ma, Johan G. Hollander, Ruta Nachane, Karoly Szuhai, Pancras C. W. Hogendoorn, Peter ten Dijke, Dipen Shah, David A. Baker   +9 more
wiley   +1 more source

Classification of Intrinsically Disordered Regions and Proteins

Chemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Peter Tompa, Peter Tompa, Benjamin Lang, M. Madan Babu, Rohit V. Pappu, Vladimir N. Uversky, Vladimir N. Uversky, Christopher J. Oldfield, Julian Gough, Marija Buljan, Richard W. Kriwacki, Gary W. Daughdrill, A. Keith Dunker, Peter E. Wright, David T. Jones, Robin van der Lee, Robin van der Lee, Philip M. Kim, Monika Fuxreiter, Robert J. Weatheritt, Joerg Gsponer   +20 more
openaire   +4 more sources