Results 91 to 100 of about 4,606,382 (149)

A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43

Advanced Science, Volume 13, Issue 56, 9 October 2026.
Phosphorylation of TAR DNA‐binding protein's 43 kDa (TDP‐43) low‐complexity domain by casein kinase 1 delta (CK1δ) acts as a molecular switch, redirecting its self‐assembly from macroscopic phase separation toward finite‐sized, spherical block‐copolymer micelles of ∼30 nm.
Rodrigo F. Dillenburg, Anastasia Lopatina, Hao Ruan, Tom Scheidt, Simone Mosna, Emre Pekbilir, Julia Bieber, Frank Schäfer‐Depoix, Katharina Landfester, Carla Schmidt, Martin M. Möckel, Svenja Morsbach, Friederike Schmid, Dorothee Dormann, Lukas Stelzl, Martin Girard, Edward A. Lemke   +16 more
wiley   +1 more source

AlphaFold2 modeling and molecular dynamics simulations of an intrinsically disordered protein.

PLoS ONE
We use AlphaFold2 (AF2) to model the monomer and dimer structures of an intrinsically disordered protein (IDP), Nvjp-1, assisted by molecular dynamics (MD) simulations.
Hao-Bo Guo, Baxter Huntington, Alexander Perminov, Kenya Smith, Nicholas Hastings, Patrick Dennis, Nancy Kelley-Loughnane, Rajiv Berry   +7 more
doaj   +1 more source

SCREENING INTERACTIONS BETWEEN PROTEINS AND DISORDERED PEPTIDES BY A NOVEL COMPUTATIONAL METHOD [PDF]

, 2013
Concerted interactions between proteins in cells form the basis of most biological processes. Biophysicists study protein–protein association by measuring thermodynamic and kinetic properties.
Zhang, Weiyi
core  

Long-lived States in an intrinsically disordered protein domain [PDF]

, 2013
Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is ...
Fernandes, L., Pons Vallès, Miquel, Kateb, F., Guerniou, C., Marín Montesinos, Ildefonso, Vasos, P. R.   +5 more
core   +1 more source

Conformationally adaptive therapeutic peptides for diseases caused by intrinsically disordered proteins (IDPs). New paradigm for drug discovery: Target the target, not the arrow

Pharmacology & Therapeutics
The traditional model of protein structure determined by the amino acid sequence is today seriously challenged by the fact that approximately half of the human proteome is made up of proteins that do not have a stable 3D structure, either partially or in totality. These proteins, called intrinsically disordered proteins (IDPs), are involved in numerous
Jacques, Fantini, Fodil, Azzaz, Coralie, Di Scala, Anaïs, Aulas, Henri, Chahinian, Nouara, Yahi   +5 more
  +6 more sources

Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide

Nature Communications
Hydrogen bonds play crucial roles in functional biomolecular dynamics. It is suggested that non-conventional hydrogen bonds engaging π electrons are prevalent in proteins. The experimental support for their existence is however limited.
Luigi Russo, Dipendu Dhar, Robin Backer, Om Prakash, Fatima Matroodi, Kerstin Overkamp, Karin Giller, Stefan Becker, Christian Griesinger, Dieter Willbold, Barbara Rossi, Mehdi D. Davari, Nasrollah Rezaei-Ghaleh   +12 more
doaj   +1 more source

Computational modeling of intrinsically disordered and phase-separated protein states

Intrinsically disordered proteins possess ensembles of conformations and lack stable three-dimensional structures. Phase separation is defined as a phenomenon in which proteins and biomolecules, often including intrinsically disordered proteins, separate
Uversky, Vladimir N., Coskuner-Weber, Orkid   +1 more
core   +1 more source

Characterisation of the effects of intrinsically disordered protein (IDP)-solvent and IDP-lipid interactions in aqueous solution and lipid monolayers

, 2019
In dieser Arbeit wurde das Aggregationsverhalten zweier verschiedener Arten intrinsisch unstrukturierter Proteine untersucht. Zum einen wurde der Temperatur-abhängige inverse Phasenübergang von thermoresponsiven Peptid-Polymeren als Funktion der Aminosäuresequenz mit Elektronenspinresonanz- Spektroskopie untersucht.
openaire   +2 more sources

Electrostatics in intrinsically disordered proteins

, 2012
Protein-protein interactions are fundamental to many biological processes. A large proportion of proteins have been identified as partially or entirely disordered in their native state.
Wong, Eric Tsz Chung
core   +1 more source

Intrinsically disordered proteins in various hypotheses on the pathogenesis of Alzheimer’xxs and Parkinson’xxs diseases

, 2019
"Dancing protein clouds: Intrinsically disordered proteins in the norm and pathology" represents a set of selected studies on a variety of research topics related to intrinsically disordered proteins.
Uversky, Vladimir N., Coşkuner Weber, Orkid   +1 more
core