AbstractProtein standard structures formed by two consecutive β-strands connected by short loops are considered in this paper. A stereochemical analysis of each standard structure has been performed to determine the necessary conditions which must be fulfilled in the amino acid sequence encoding the standard structure. It is shown that amino acid sequences coding for the same standard structure in ditterent proteins have practically the same order of hydrophobic, hydrophilic and glycine residues. The results of the stereochemical analysis are confirmed by a large number of examples from known protein structures
We seek to understand the interplay between amino acid sequence and local structure in proteins. Are...
Two quantities, herein defined as the displacement and the uniqueness, describe quantitatively the t...
A computer-readable dictionary for protein structure refinement is presented. The dictionary is base...
A total of 51 polypeptides of known amino acid sequence and secondary structure have been screened f...
The search for amino acid sequence homologies can be a powerful tool for predicting protein structur...
The problem of structural similarity of polypeptide chains of low sequence similarity representing a...
Proteins are very complex physical objects consisting of thousands of atoms and hundreds of amino ac...
The fact that amino acid sequences dictate the tertiary structures of proteins has been known for mo...
The flexibility of the polypeptide fold of proteins is essentially due to the rotational freedom abo...
Proteins in nature exhibit special properties including high regularity in structure and high correl...
International audienceWe present a thorough analysis of the relation between amino acid sequence and...
This paper reports an extensive sequence analysis of the α-helices of proteins, α-Helices were extra...
Using the data from Protein Data Bank the correlations of primary and secondary structures of protei...
AbstractA secondary structure prediction algorithm is proposed on the hypothesis that short homologo...
The flexibility of the polypeptide fold of proteins is essentially due to the rotational freedom abo...
We seek to understand the interplay between amino acid sequence and local structure in proteins. Are...
Two quantities, herein defined as the displacement and the uniqueness, describe quantitatively the t...
A computer-readable dictionary for protein structure refinement is presented. The dictionary is base...
A total of 51 polypeptides of known amino acid sequence and secondary structure have been screened f...
The search for amino acid sequence homologies can be a powerful tool for predicting protein structur...
The problem of structural similarity of polypeptide chains of low sequence similarity representing a...
Proteins are very complex physical objects consisting of thousands of atoms and hundreds of amino ac...
The fact that amino acid sequences dictate the tertiary structures of proteins has been known for mo...
The flexibility of the polypeptide fold of proteins is essentially due to the rotational freedom abo...
Proteins in nature exhibit special properties including high regularity in structure and high correl...
International audienceWe present a thorough analysis of the relation between amino acid sequence and...
This paper reports an extensive sequence analysis of the α-helices of proteins, α-Helices were extra...
Using the data from Protein Data Bank the correlations of primary and secondary structures of protei...
AbstractA secondary structure prediction algorithm is proposed on the hypothesis that short homologo...
The flexibility of the polypeptide fold of proteins is essentially due to the rotational freedom abo...
We seek to understand the interplay between amino acid sequence and local structure in proteins. Are...
Two quantities, herein defined as the displacement and the uniqueness, describe quantitatively the t...
A computer-readable dictionary for protein structure refinement is presented. The dictionary is base...