A formidable challenge in molecular biology is the prediction of the three-dimensional structures of the native state of proteins from their sequence of amino acids. An essential step to solve this problem is the extraction of the coarse-grained interaction potentials between the amino acids. Here we outline preliminary results of a strategy that accomplishes such goal with the search of those potentials which are able to recognize the native state of a protein as a stable local minimum. The method is implemented by exploiting several numerical and analytical tools which have been recently developed by our group. The results are extremely promising: despite the fact that we have used simple forms for Hamiltonians, the extracted potentials a...
For 238 mutations of residues totally or partially buried in the protein core, we estimate the foldi...
The idea of using empirical amino acid-pair-potentials extracted from proteins of known structure in...
We present and discuss a novel approach to the direct and inverse protein folding problem. The propo...
A formidable challenge in molecular biology is the prediction of the three-dimensional structures of...
A formidable challenge in molecular biology is the prediction of the three-dimensional structure...
The prediction of the three-dimensional structures of the native states of proteins from the seq...
The prediction of the three-dimensional structures of the native states of proteins from the sequenc...
The prediction of the three-dimensional structures of the native states of proteins from the sequenc...
We outline a general strategy for determining the effective coarse-grained interactions between the ...
We discuss methods for the determination of the effective pairwise interactions between amino acids ...
We discuss methods for the determination of the effective pairwise interactions between amino ac...
We propose a novel method for the determination of the effective interaction potential between the a...
. A smooth empirical potential is constructed for use in off-lattice protein folding studies. Our po...
Under appropriate physiological conditions, proteins fold into their biologically active native conf...
An effective potential function is critical for protein structure prediction and folding simulation....
For 238 mutations of residues totally or partially buried in the protein core, we estimate the foldi...
The idea of using empirical amino acid-pair-potentials extracted from proteins of known structure in...
We present and discuss a novel approach to the direct and inverse protein folding problem. The propo...
A formidable challenge in molecular biology is the prediction of the three-dimensional structures of...
A formidable challenge in molecular biology is the prediction of the three-dimensional structure...
The prediction of the three-dimensional structures of the native states of proteins from the seq...
The prediction of the three-dimensional structures of the native states of proteins from the sequenc...
The prediction of the three-dimensional structures of the native states of proteins from the sequenc...
We outline a general strategy for determining the effective coarse-grained interactions between the ...
We discuss methods for the determination of the effective pairwise interactions between amino acids ...
We discuss methods for the determination of the effective pairwise interactions between amino ac...
We propose a novel method for the determination of the effective interaction potential between the a...
. A smooth empirical potential is constructed for use in off-lattice protein folding studies. Our po...
Under appropriate physiological conditions, proteins fold into their biologically active native conf...
An effective potential function is critical for protein structure prediction and folding simulation....
For 238 mutations of residues totally or partially buried in the protein core, we estimate the foldi...
The idea of using empirical amino acid-pair-potentials extracted from proteins of known structure in...
We present and discuss a novel approach to the direct and inverse protein folding problem. The propo...