Advantages of proteins being disordered
Z Liu, Y Huang - Protein Science, 2014 - Wiley Online Library
The past decade has witnessed great advances in our understanding of protein structure‐
function relationships in terms of the ubiquitous existence of intrinsically disordered proteins …
function relationships in terms of the ubiquitous existence of intrinsically disordered proteins …
Cooperativity, local-nonlocal coupling, and nonnative interactions: principles of protein folding from coarse-grained models
Coarse-grained, self-contained polymer models are powerful tools in the study of protein
folding. They are also essential to assess predictions from less rigorous theoretical …
folding. They are also essential to assess predictions from less rigorous theoretical …
Kinetic advantage of intrinsically disordered proteins in coupled folding–binding process: a critical assessment of the “fly-casting” mechanism
Y Huang, Z Liu - Journal of molecular biology, 2009 - Elsevier
Intrinsically disordered proteins (IDPs) are recognized to play important roles in many
biological functions such as transcription and translation regulation, cellular signal …
biological functions such as transcription and translation regulation, cellular signal …
Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation
The pathology of Alzheimer's disease is connected to the aggregation of β-amyloid (Aβ)
peptide, which in vivo exists as a number of length-variants. Truncations and extensions are …
peptide, which in vivo exists as a number of length-variants. Truncations and extensions are …
Limiting the valence: advancements and new perspectives on patchy colloids, soft functionalized nanoparticles and biomolecules
Limited bonding valence, usually accompanied by well-defined directional interactions and
selective bonding mechanisms, is nowadays considered among the key ingredients to …
selective bonding mechanisms, is nowadays considered among the key ingredients to …
N-terminal extensions retard Aβ42 fibril formation but allow cross-seeding and coaggregation with Aβ42
O Szczepankiewicz, B Linse, G Meisl… - Journal of the …, 2015 - ACS Publications
Amyloid β-protein (Aβ) sequence length variants with varying aggregation propensity coexist
in vivo, where coaggregation and cross-catalysis phenomena may affect the aggregation …
in vivo, where coaggregation and cross-catalysis phenomena may affect the aggregation …
Computational protein design: a review
I Coluzza - Journal of Physics: Condensed Matter, 2017 - iopscience.iop.org
Proteins are one of the most versatile modular assembling systems in nature.
Experimentally, more than 110 000 protein structures have been identified and more are …
Experimentally, more than 110 000 protein structures have been identified and more are …
Casein structures in the context of unfolded proteins
Caseins were among the first proteins to be recognised as functional but unfolded. Many
others are now known, providing better models of casein behaviour than either detergents or …
others are now known, providing better models of casein behaviour than either detergents or …
[HTML][HTML] The functional roles of the unstructured N-and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins
Small heat-shock proteins (sHsps), such as αB-crystallin, are one of the major classes of
molecular chaperone proteins. In vivo, under conditions of cellular stress, sHsps are the …
molecular chaperone proteins. In vivo, under conditions of cellular stress, sHsps are the …
A simple lattice model that captures protein folding, aggregation and amyloid formation
The ability of many proteins to convert from their functional soluble state to amyloid fibrils
can be attributed to inter-molecular beta strand formation. Such amyloid formation is …
can be attributed to inter-molecular beta strand formation. Such amyloid formation is …