Linking folding and binding
PE Wright, HJ Dyson - Current opinion in structural biology, 2009 - Elsevier
Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part,
upon binding to their physiological targets. The past few years have seen an exponential …
upon binding to their physiological targets. The past few years have seen an exponential …
Principles of protein− protein interactions: what are the preferred ways for proteins to interact?
Proteins are the working horse of the cellular machinery. They are responsible for diverse
functions ranging from molecular motors to signaling. They catalyze reactions, transport …
functions ranging from molecular motors to signaling. They catalyze reactions, transport …
Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell
All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …
Natively unfolded proteins
AL Fink - Current opinion in structural biology, 2005 - Elsevier
It is now clear that a significant fraction of eukaryotic genomes encode proteins with
substantial regions of disordered structure. In spite of the lack of structure, these proteins …
substantial regions of disordered structure. In spite of the lack of structure, these proteins …
Protein dynamics and conformational disorder in molecular recognition
Recognition requires protein flexibility because it facilitates conformational rearrangements
and induced‐fit mechanisms upon target binding. Intrinsic disorder is an extreme on the …
and induced‐fit mechanisms upon target binding. Intrinsic disorder is an extreme on the …
[BOOK][B] Structure and function of intrinsically disordered proteins
The existence and functioning of intrinsically disordered proteins (IDPs) challenge the
classical structure-function paradigm that equates function with a well-defined 3D structure …
classical structure-function paradigm that equates function with a well-defined 3D structure …
On the specificity of protein–protein interactions in the context of disorder
With the increased focus on intrinsically disordered proteins (IDPs) and their large
interactomes, the question about their specificity—or more so on their multispecificity—arise …
interactomes, the question about their specificity—or more so on their multispecificity—arise …
Collapse transitions of proteins and the interplay among backbone, sidechain, and solvent interactions
Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like
conformations. Additionally, they can fold into well-defined three-dimensional structures or …
conformations. Additionally, they can fold into well-defined three-dimensional structures or …
Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins
Diffusion measurements by pulsed-field gradient NMR and fluorescence correlation
spectroscopy can be used to probe the hydrodynamic radius of proteins, which contains …
spectroscopy can be used to probe the hydrodynamic radius of proteins, which contains …
[HTML][HTML] Receptor-activated transcription factors and beyond: multiple modes of Smad2/3-dependent transmission of TGF-β signaling
K Miyazawa, Y Itoh, H Fu, K Miyazono - Journal of Biological Chemistry, 2024 - Elsevier
Transforming growth factor β (TGF-β) is a pleiotropic cytokine that is widely distributed
throughout the body. Its receptor proteins, TGF-β type I and type II receptors, are also …
throughout the body. Its receptor proteins, TGF-β type I and type II receptors, are also …