Tandem-repeat proteins differ from globular proteins, both in their biophysical characteristics and in how they interact with their respective partners, yet they comprise nearly one third of the human proteome and are central to many cellular processes and disease phenotypes. Repeat proteins have been shown to behave like nano-sized biological springs: they are flexible, dynamic and elastic. Using coarse-grained models, I discuss how intrinsic flexibility may arise in repeat proteins and how it could be crucial for the biological function of two systems: PR65, the scaffold protein of the protein phosphatase 2A, and Rap proteins, which are involved in quorum sensing. To interrogate α-solenoids at physiologically relevant forces, I performed ...
For thousands of years, nature has selected and perfected the conformation foldings of its molecular...
AbstractSingle-molecule manipulation techniques have enabled the characterization of the unfolding a...
Single-molecule atomic force spectroscopy probes elastic properties of proteins such as titin and ub...
In contrast to globular proteins, the structure of repeat proteins is dominated by a regular set of ...
In contrast to globular proteins, the structure of repeat proteins is dominated by a regular set of ...
In this chapter we review recent studies of repeat proteins, a class of proteins consisting of tande...
Tandem-repeat proteins comprise small secondary structure motifs that stack to form one- dimensional...
Studying protein folding and protein design in globular proteins presents significant challenges bec...
A central question in protein evolution is the extent to which naturally occurring proteins sample t...
Understanding the molecular mechanism of protein folding has always remained a challenging problem. ...
Topological defects in highly repetitive structural proteins strongly affect their mechanical proper...
Although they are widely distributed across kingdoms and are involved in a myriad of essential proce...
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
Interplay between mechanical forces and chemical transformations is fundamental to the strength of m...
Mechanical unfolding and refolding may regulate the molecular elasticity of modular proteins with me...
For thousands of years, nature has selected and perfected the conformation foldings of its molecular...
AbstractSingle-molecule manipulation techniques have enabled the characterization of the unfolding a...
Single-molecule atomic force spectroscopy probes elastic properties of proteins such as titin and ub...
In contrast to globular proteins, the structure of repeat proteins is dominated by a regular set of ...
In contrast to globular proteins, the structure of repeat proteins is dominated by a regular set of ...
In this chapter we review recent studies of repeat proteins, a class of proteins consisting of tande...
Tandem-repeat proteins comprise small secondary structure motifs that stack to form one- dimensional...
Studying protein folding and protein design in globular proteins presents significant challenges bec...
A central question in protein evolution is the extent to which naturally occurring proteins sample t...
Understanding the molecular mechanism of protein folding has always remained a challenging problem. ...
Topological defects in highly repetitive structural proteins strongly affect their mechanical proper...
Although they are widely distributed across kingdoms and are involved in a myriad of essential proce...
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
Interplay between mechanical forces and chemical transformations is fundamental to the strength of m...
Mechanical unfolding and refolding may regulate the molecular elasticity of modular proteins with me...
For thousands of years, nature has selected and perfected the conformation foldings of its molecular...
AbstractSingle-molecule manipulation techniques have enabled the characterization of the unfolding a...
Single-molecule atomic force spectroscopy probes elastic properties of proteins such as titin and ub...