The formation of disulphide bridges between cysteines plays an important role in protein
folding, structure, function, and evolution. Here, we develop new methods for predicting …

The formation of disulphide bridges among cysteines is an important fea-ture of protein
structures. Here we develop new methods for the predic-tion of disulphide bond connectivity …

Motivation: We focus on the prediction of disulfide bridges in proteins starting from their
amino acid sequence and from the knowledge of the disulfide bonding state of each …

Disulfide bridges stabilize protein structures covalently and play an important role in protein
folding. Predicting disulfide connectivity precisely helps towards the solution of protein …

Motivation: We describe a stand-alone algorithm to predict disulfide bond partners in a
protein given only the amino acid sequence, using a novel neural network architecture (the …

Disulfide bonds are primary covalent cross‐links formed between two cysteine residues in
the same or different protein polypeptide chains, which play important roles in the folding …

Motivation: A major problem in protein structure predictionis the correct location of disulfide
bridges in cysteine-rich proteins. In protein-folding prediction, the location of disulfide …

Motivation: Cysteine-rich proteins cover many important families in nature but there are
currently no methods specifically designed for modeling the structure of these proteins. The …

Correctly predicting the disulfide bond topology in a protein is of crucial importance for the
understanding of protein function and can be of great help for tertiary prediction methods …

Motivation: Prediction of disulfide bond connectivity facilitates structural and functional
annotation of proteins. Previous studies suggest that cysteines of a disulfide bond mutate in …