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Figure 16: Various Features at the Protherm Site.<br />
Figure 17: Various features of Protherm Version 3.0. Figure 18: List of Important Information for Prote<strong>in</strong> Fold<strong>in</strong>g Experiment at Prote<strong>in</strong> Fold<strong>in</strong>g<br />
Database (Pfd).<br />
Prote<strong>in</strong> Fold<strong>in</strong>g Database (Pfd)<br />
It is really an <strong>in</strong>formative, easily accessible and <strong>in</strong>novative resource and database that facilitates prote<strong>in</strong> fold<strong>in</strong>g data of more than<br />
50 different prote<strong>in</strong>s belongs to various families. Data of structural, k<strong>in</strong>etic as well as thermodynamic <strong>in</strong> nature is available on prote<strong>in</strong><br />
fold<strong>in</strong>g database that could be accessed through web platform. With the various useful features it l<strong>in</strong>ks with the other prote<strong>in</strong> databases<br />
as well [27].<br />
Prote<strong>in</strong> Fold<strong>in</strong>g Database 2.0 provides freely accessible and centralized data repository. It has been built as a comparative repository<br />
provid<strong>in</strong>g k<strong>in</strong>etic and thermodynamic features for the fold<strong>in</strong>g of prote<strong>in</strong> <strong>in</strong> a useful and user friendly way [27].<br />
Site Directed Mutator (Sdm)<br />
SDM is a server for predict<strong>in</strong>g effects of mutations on prote<strong>in</strong> stability and malfunction. Site Directed Mutator is a statistical potential<br />
energy function that exercises environment-specific am<strong>in</strong>o-acid replacement frequencies with<strong>in</strong> homologous prote<strong>in</strong> families to compute<br />
a stability score, which is correspond<strong>in</strong>g to the free energy difference between the wild-type and mutant prote<strong>in</strong> [28].<br />
SRide<br />
SRide server provides data that could be employed for the calculation of van der Waals atomic radius among the am<strong>in</strong>o acids. The<br />
residues present <strong>in</strong> the polypeptide and play a crucial role for the stability of prote<strong>in</strong> molecules are called stabiliz<strong>in</strong>g residues (SRs).<br />
These residues are selected by us<strong>in</strong>g various methods like <strong>in</strong>teraction of a given residue with its neighbor<strong>in</strong>g residues and observ<strong>in</strong>g the<br />
evolutionary conservation <strong>in</strong> the prote<strong>in</strong> structures [29].<br />
OMICS Group eBooks<br />
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