Predicting substitutions to modulate disorder and stability in coiled-coils
Background Coiled-coils are described as stable structural motifs, where two or more
helices wind around each other. However, coiled-coils are associated with local mobility and …
helices wind around each other. However, coiled-coils are associated with local mobility and …
[PDF][PDF] Predicting substitutions to modulate disorder and stability in
EL Longhi, A Carbone - hal.science
Coiled-coils are described as stable structural motifs, where two or more helices wind
around each 15 other. However, coiled-coils are associated with local mobility and intrinsic …
around each 15 other. However, coiled-coils are associated with local mobility and intrinsic …
Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints
Coiled-coil proteins provide an excellent scaffold for multi-state de novo protein design due
to their established sequence-to-structure relationships and ability to switch conformations in …
to their established sequence-to-structure relationships and ability to switch conformations in …
Discrete molecular dynamics can predict helical prestructured motifs in disordered proteins
D Szöllősi, T Horvath, KH Han, NV Dokholyan… - PLoS …, 2014 - journals.plos.org
Intrinsically disordered proteins (IDPs) lack a stable tertiary structure, but their short binding
regions termed Pre-Structured Motifs (PreSMo) can form transient secondary structure …
regions termed Pre-Structured Motifs (PreSMo) can form transient secondary structure …
Computational assessment of folding energy landscapes in heterodimeric coiled coils
The coiled coil structural motif consists of alpha helices supercoiling around each other to
form staggered knobs‐into‐holes packing. Such structures are deceptively simple …
form staggered knobs‐into‐holes packing. Such structures are deceptively simple …
Simulation of coupled folding and binding of an intrinsically disordered protein in explicit solvent with metadynamics
M Han, J Xu, Y Ren, J Li - Journal of Molecular Graphics and Modelling, 2016 - Elsevier
The C-terminal domain of measles virus nucleoprotein is an intrinsically disordered protein
that could bind to the X domain (XD) of phosphoprotein P to exert its physiological function …
that could bind to the X domain (XD) of phosphoprotein P to exert its physiological function …
Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model
TR Sisk, P Robustelli - … of the National Academy of Sciences, 2024 - National Acad Sciences
A central challenge in the study of intrinsically disordered proteins is the characterization of
the mechanisms by which they bind their physiological interaction partners. Here, we utilize …
the mechanisms by which they bind their physiological interaction partners. Here, we utilize …
Exploring alternate states and oligomerization preferences of coiled‐coils by de novo structure modeling
Homomeric coiled‐coils can self‐assemble into a wide range of structural states with
different helix topologies and oligomeric states. In this study, we have combined de novo …
different helix topologies and oligomeric states. In this study, we have combined de novo …
Assessing the helical stability of polyXYs at the boundaries of Intrinsically Disordered Regions with MD simulations
M Goncalves-Kulik, LA Baptista, F Schmid, M Andrade - bioRxiv, 2024 - biorxiv.org
Intrinsically disordered regions (IDRs) in proteins lack stable structure. By carrying many
hydrophilic and charged residues, it prevents them from forming globular domains and …
hydrophilic and charged residues, it prevents them from forming globular domains and …
AlphaFold with conformational sampling reveals the structural landscape of homorepeats
Homorepeats are motifs with reiterations of the same amino acid. They are prevalent in
proteins associated with diverse physiological functions but also linked to several …
proteins associated with diverse physiological functions but also linked to several …