User:Eric Martz/Introduction to Structural Bioinformatics I: Difference between revisions
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Try out the first six views (links) at the upper left, and any other controls that interest you. In particular, we will use these capabilities of ''FirstGlance'' in the Powerpoint report: | Try out the first six views (links) at the upper left, and any other controls that interest you. In particular, we will use these capabilities of ''FirstGlance'' in the Powerpoint report: | ||
:A. Hydrophobic/Polar. Water-soluble proteins have polar/charged amino acids nearly everywhere on their surfaces (Examples: small [[2hhd]], large [[1igy]]). Large hydrophobic surface areas may indicate transmembrane proteins (insoluble; example: [[1bl8]]). | :A. Hydrophobic/Polar. | ||
*Water-soluble proteins have polar/charged amino acids nearly everywhere on their surfaces (Examples: small [[2hhd]], large [[1igy]]). Patches of hydrophobic amino acids on the surfaces of soluble proteins are usually less than ~10 å in their smaller diameter, and usually recessed. | |||
*Hydrophobic surface patches may be buried in chain-to-chain contacts -- check the [[#Section_6:_Biological_Unit|biological unit]] (example: [[Lac_repressor#Structure_of_the_lac_repressor|lac repressor homodimer]]). | |||
*Large, protruding hydrophobic surface areas (>25 Å in their smaller diameter) may indicate transmembrane proteins (insoluble; example: [[1bl8]]). | |||
==Powerpoint Report== | ==Powerpoint Report== | ||