Per-residue predictors (such as the PONDR® group of predictors) output a score for each residue in a protein and are especially useful when applied to proteins having both structured and disordered regions.
Jpred 3 and DisEMBL were used to perform, respectively, secondary structure and disorder predictions.
Changes in secondary structure and disorder predictions were linearly proportional to the change in sequence.
Our analyses of regular secondary structure and disorder are based on very different datasets.
Therefore, understanding how structure and disorder work together will be crucial for uncovering the full extent of protein function.
This preliminary structure, as well as sequence-based secondary structure and disorder prediction confirmed the presence of three compact α/β domains separated by flexible linkers.
To tackle these questions, we in silico mutated native protein sequences into random sequence-like ensembles and monitored the change in predicted secondary structure and disorder.
These methods are capable of detecting secondary structure and disorder from sequence information alone, with a reasonable degree of accuracy [benchmarked ∼80% (21, 22)].
Do random sequences have different content in secondary structure and disorder than native proteins that have evolved to satisfy many constraints?
