Globular Proteins: Difference between revisions

Disulfide bonds and metal ion chelates can stabilize the tertiary structure in the absence of well organized layers which generate hydrophobic attractions.  Some proteins are small in size and therefore do not have large amounts of backbone that can be organized into layers.  Others have significant backbone, but the layers are not well organized and therefore are non-stabilizing.  The attractions formed by metal ions chelates or disulfide bonds in these proteins are as important or more so than the hydrophobic interactions of the organized layers.  Some proteins are intrinsically unstructured.  They do have secondary structure, but these structural components are not extensively folded back on themselves resulting in a more extended conformation. With this extended conformation these proteins do not have binding pockets normally found in globular proteins so as a consequence binding to these proteins occurs over a relatively large surface area.