Protein Investigator Explore protein structure fast and easy.
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Protein Investigator Ranking & Summary

Protein Investigator Tags

view display explore protein retrieve protein analyze protein explore information structure Protein Synthesizer view protein structure display protein structure protein crystallization protein translocation protein visualization explore structure protein extraction protein structures refinement protein structure regulated protein valudation validate regulated protein Protein Viewer Protein Test Protein Residue Protein Browser explore protein structure view protein Visualize Protein Protein Interaction protein vizualizer protein 3D structure

Protein Investigator Description

Many lab exercises use molecular visualization software that allows students to to 'see' a protein in its full 3-dimensional form and to make hypotheses about the interactions between various side chains. However, these programs do not allow students to test their hypotheses because molecular visualization software does not allow students to make changes to the protein sequence and observe their effects on the protein's structure and function. Protein Investigator is a very useful tool designed to give users an opportunity to interactively explore protein structure and function in a simplified system. This is a highly-simplified model of protein folding. It is not intended to predict the correct structures of any proteins; it is designed to illustrate the major principles involved in that process. Main features: Amino acids have side-chains of varying hydrophobicity, charge, and hydrogen bonding capacity. The amino acids a reconnected in an un-branched chain that can bend. Hydrophobic amino acids will tend to avoid the water that surrounds the protein; hydrophilic amino acids will bind to the water. Amino acids that can form hydrogen bonds will tend to form hydrogen bonds if they can. Positively-charged amino acids will tend to form ionic bonds with negatively-charged amino acids if they can. Like-charged amino acids will repel each other if they can. Ionic interactions are stronger than hydrogen bonds, which are stronger than hydrophobic interactions. Proteins can be folded under oxidizing (Disulfide Bonds ON) or reducing (Disulfide Bonds OFF) conditions.

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