Structural, dynamic and energetic properties of proteins in solution can be studied in atomic detail by molecular dynamics computer simulation. Protein unfolding can be caused by a variety of driving forces induced in different ways: increased temperature or pressure, change of solvent composition, or protein amino acid mutation. The stability and unfolding of four different proteins (bovine pancreatic trypsin inhibitor, hen egg white lysozyme, the surfactant protein C and the DNA-binding domain of the 434 repressor) have been studied by applying the afore-mentioned driving forces and also to some artificial forces. The results give a picture of protein (in)stability and possible unfolding pathways, and are compared to experimental data whe...
The relative stability of protein structures determined by either X-ray crystallography or nuclear m...
We have employed a Hamiltonian model based on a self-consistent Gaussian appoximation to examine the...
Protein stability is the net balance of forces, determining whether a protein will be in its native ...
Four methods are compared to drive the unfolding of a protein: (1) high temperature (T-run), (2) hig...
We have performed molecular dynamics simulations for a total duration of more than 10 ls (with most ...
Single-molecule experiments and their application to probe the mechanical resistance and related pro...
The folded native structure of a protein is highly sensitive towards the nature of solvent under spe...
BBA1 is a designed protein that has only 23 residues. It is the smallest protein without disulfide b...
AbstractIn the last decade atomic force microscopy has been used to measure the mechanical stability...
The relative stability of protein structures determined by either X-ray crystallography or nuclear m...
AbstractSingle-molecule manipulation techniques have enabled the characterization of the unfolding a...
Molecular dynamics simulations of the DNA binding domain of 434 repressor are presented which aim at...
This paper describes computer modelling studies using classical Molecular Dynamics techniques and th...
Single molecule 'force spectroscopy' techniques (e.g., atomic force microscopy) that measure the for...
Abstract:- This paper describes computer modelling studies using classical Molecular Dynamics techni...
The relative stability of protein structures determined by either X-ray crystallography or nuclear m...
We have employed a Hamiltonian model based on a self-consistent Gaussian appoximation to examine the...
Protein stability is the net balance of forces, determining whether a protein will be in its native ...
Four methods are compared to drive the unfolding of a protein: (1) high temperature (T-run), (2) hig...
We have performed molecular dynamics simulations for a total duration of more than 10 ls (with most ...
Single-molecule experiments and their application to probe the mechanical resistance and related pro...
The folded native structure of a protein is highly sensitive towards the nature of solvent under spe...
BBA1 is a designed protein that has only 23 residues. It is the smallest protein without disulfide b...
AbstractIn the last decade atomic force microscopy has been used to measure the mechanical stability...
The relative stability of protein structures determined by either X-ray crystallography or nuclear m...
AbstractSingle-molecule manipulation techniques have enabled the characterization of the unfolding a...
Molecular dynamics simulations of the DNA binding domain of 434 repressor are presented which aim at...
This paper describes computer modelling studies using classical Molecular Dynamics techniques and th...
Single molecule 'force spectroscopy' techniques (e.g., atomic force microscopy) that measure the for...
Abstract:- This paper describes computer modelling studies using classical Molecular Dynamics techni...
The relative stability of protein structures determined by either X-ray crystallography or nuclear m...
We have employed a Hamiltonian model based on a self-consistent Gaussian appoximation to examine the...
Protein stability is the net balance of forces, determining whether a protein will be in its native ...