1.4 A RMSd.ġjbl PEP-FOLD best model (cyan) and native (green) conformations. PEP-FOLD latest evolution improves performance for linear peptides up to 36 amino acids - best model with an averaged RMSd of 2.1 A from NMR structure, also allows user specified constraints such as disulfide bonds and inter-residue proximities.ġwqc PEP-FOLD best model (cyan) and experimental (green) conformations. Use this service for such constrained peptides. Not optimized yet for disulfide bonds or user specified constraints. Faster, open for linear peptides in solution from 5 up to 50 amino acids, allows preliminary peptide protein interaction studies. What's new: Jan 2016: PEP-FOLD3 is on-line.
Predicted series of SA letters to a greedy algorithm and aĬoarse-grained force field. This method,īased on structural alphabet SA letters to describe theĬonformations of four consecutive residues, couples the Peptide structures from amino acid sequences. PEP-FOLD is a de novo approach aimed at predicting Welcome to the PEP-FOLD 2011 improved service!
0 kommentar(er)
