Sequencing, proteins data evaluation

The ExPASy server (www.expasy.chl is one of the most useful servers, where almost any bioinforma tic tool can be found, together with useful links to other websites such as NCBI or EBI. The several access databases are descriptive, easy to follow, and up to date. Protein data bank searches with SwissProt or Trembl, as well as sequence alignments using either SimAlign (for two sequences) or ClustalW (for more than two protein sequences) can be started from ExPASy, to name just a few of the possibilities available. Access is also given to the Roche Applied Science Biochemical pathways where either keyword searches for particular enzymes or for metabolites can be performed, or entire metabolic pathways or sections thereof can be visualized. Proteomics evaluation is also available on ExPASy, which features free 2D-PAGE software called Melanie. 

Milik et al. (1995) developed a neural network system to evaluate side-chain packing in protein structures. Instead of using protein sequence as input to the neural network as in most other studies, protein structure represented by a side-chain-side-chain contact map was used. Contact maps of globular protein structures in the Protein Data Bank were scanned using 7x7 windows, and converted to 49 binary numbers for the neural network input. One output unit was used to determine whether the contact pattern is popular in... 

Clinical evaluation and material collection —> ELISA microarray —> Protein sequencing — Data mining tools <-> Drug Discovery... 

The Association of Biomolecular Resource Facilities (ABRP) Protein Sequence Research Committee was established in 1988 in order to provide individual laboratories with a means of self-evaluation. Each year test samples have been distributed, enabling laboratories an opportunity to monitor their performance in areas such as sample handling, insuument operation/optimization, and data interpretation. In previous years these samples have focused on sensitivity of protein sequencing (1, 6), sample heterogeneity (2, 8), protein-bound peptides on PVDF membrane or in solution (3, 4), post-translational modifications (5), identification of cysteine and tryptophan (7), and length of sequence assignment (8). 

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