Results 71 to 80 of about 3,579,241 (217)

Mechanisms 
of
 change 
in 
protein 
architecture [PDF]

open access: yes, 2011
Proteins are the basic building blocks and functional units in all living organisms. Moreover, differences between species can frequently be explained with differences in their protein complements.

core   +2 more sources

Stabilization Effect of Intrinsically Disordered Regions on Multidomain Proteins: The Case of the Methyl-CpG Protein 2, MeCP2

open access: yesBiomolecules, 2021
Intrinsic disorder plays an important functional role in proteins. Disordered regions are linked to posttranslational modifications, conformational switching, extra/intracellular trafficking, and allosteric control, among other phenomena.
David Ortega-Alarcon   +6 more
doaj   +1 more source

Long-Range Entropic Effects on Protein Intrinsically Disordered Regions [PDF]

open access: yes, 2019
Entropy calculations represent one of the most challenging steps in obtaining the binding free energy in proteins and their complexes, which is a grand challenge in computational biology.
Agnieszka K., Bronowska   +3 more
core   +1 more source

Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments

open access: yesFrontiers in Molecular Biosciences, 2019
Intrinsically disordered proteins (IDPs) represent a structural class of proteins that do not have a well-defined, 3D fold in solution, and often have little secondary structure.
Steffen P. Graether
doaj   +1 more source

AlphaFold2 models indicate that protein sequence determines both structure and dynamics

open access: yesScientific Reports, 2022
AlphaFold 2 (AF2) has placed Molecular Biology in a new era where we can visualize, analyze and interpret the structures and functions of all proteins solely from their primary sequences. We performed AF2 structure predictions for various protein systems,
Hao-Bo Guo   +12 more
doaj   +1 more source

Intrinsically Disordered Proteins (IDPs): Experimental and Computational Approaches in Drug Discovery [PDF]

open access: yesDrug Designing & Intellectual Properties International Journal, 2018
Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as Parkinson disease, Alzheimer disease, diabetes, and so on.
openaire   +1 more source

Diverging Liquid–Liquid Phase Separation Behavior of Different Recombinant Major Ampullate Spidroins

open access: yesAdvanced Science, EarlyView.
Fibers spun from the MaSp1‐derivative as well as MaSp1‐MaSp2‐mixtures provide a deeper insight into the assembly process of the spidroins and how hierarchical architectures of spider silk fibers could be achieved. ABSTRACT Spider silk fibers show exceptional mechanical properties, based on their underlying spider silk proteins (spidroins) as well as a ...
Tim Schiller   +2 more
wiley   +1 more source

IDP-Bert: Predicting Properties of Intrinsically Disordered Proteins Using Large Language Models

open access: yesThe Journal of Physical Chemistry B
22 pages, 5 ...
Parisa Mollaei   +3 more
openaire   +3 more sources

Dynamics of proteins with different molecular structures under solution condition

open access: yesScientific Reports, 2020
Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-established ...
Rintaro Inoue   +12 more
doaj   +1 more source

α‐Synuclein Forms Distinct Micelle‐Like Assemblies at Low Ionic Strengths

open access: yesAdvanced Science, EarlyView.
At high ionic strength, α‐synuclein forms diverse assemblies, including oligomers, fibrils, and condensates. Here, we show that at low ionic strength, α‐synuclein adopts a distinct, low‐abundance assembly state. These assemblies maintain a constant size above a critical concentration and do not coalesce, suggesting a micelle‐like organization ...
Sophie Hertel   +10 more
wiley   +1 more source

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