to ime in ging n e G6 the ldin jor wa enc ns roles of cofactors in the functions of these proteins, but may also offer new insights into understanding of the binding mechanisms. Therefore, using single-molecule methodologies to directly probe different conformers during monitor the kinetics of protein folding and its cofactor AFM can readily monitor the evolution of different protein conformers during the folding of proteins in the presenc
While single-molecule force spectroscopy has greatly advanced the study of protein folding, there ar...
Single molecule experiments provide insight into the individuality of biological macromolecules, the...
Proteins are intrinsically dynamic, sampling numerous conformations. For example, they may transitio...
AbstractMany proteins in living cells require cofactors to carry out their biological functions. To ...
Traditionally, protein-protein adhesion interactions have been studied in reversible equilibrium con...
Exhibiting low-energy (un)folding barriers and fast kinetics, ultrafast folding proteins are enticin...
The advent of advanced single molecule measurements unveiled a great wealth of dynamic information r...
© 2012 Elsevier Inc. All rights reserved.Atomic force microscopy (AFM) applied to biological systems...
Single-molecule spectroscopy has developed into an important method for probing protein structure an...
Advances in single-molecule manipulation techniques have recently enabled researchers to study a gro...
AbstractProtein–ligand interactions are ubiquitous and play important roles in almost every biologic...
Single-molecule force spectroscopy sheds light onto the free energy landscapes governing protein fol...
Single molecule experiments provide insight into the individuality of biological macromolecules, the...
Single-molecule force spectroscopy is a powerful tool for studying protein folding. Over the last de...
The work presented in this dissertation focuses on the kinetics of biomolecular reactions under mech...
While single-molecule force spectroscopy has greatly advanced the study of protein folding, there ar...
Single molecule experiments provide insight into the individuality of biological macromolecules, the...
Proteins are intrinsically dynamic, sampling numerous conformations. For example, they may transitio...
AbstractMany proteins in living cells require cofactors to carry out their biological functions. To ...
Traditionally, protein-protein adhesion interactions have been studied in reversible equilibrium con...
Exhibiting low-energy (un)folding barriers and fast kinetics, ultrafast folding proteins are enticin...
The advent of advanced single molecule measurements unveiled a great wealth of dynamic information r...
© 2012 Elsevier Inc. All rights reserved.Atomic force microscopy (AFM) applied to biological systems...
Single-molecule spectroscopy has developed into an important method for probing protein structure an...
Advances in single-molecule manipulation techniques have recently enabled researchers to study a gro...
AbstractProtein–ligand interactions are ubiquitous and play important roles in almost every biologic...
Single-molecule force spectroscopy sheds light onto the free energy landscapes governing protein fol...
Single molecule experiments provide insight into the individuality of biological macromolecules, the...
Single-molecule force spectroscopy is a powerful tool for studying protein folding. Over the last de...
The work presented in this dissertation focuses on the kinetics of biomolecular reactions under mech...
While single-molecule force spectroscopy has greatly advanced the study of protein folding, there ar...
Single molecule experiments provide insight into the individuality of biological macromolecules, the...
Proteins are intrinsically dynamic, sampling numerous conformations. For example, they may transitio...