sheets polypeptide chains folded into a spherical or globular shape consists of a single type of secondary structure contain several types of secondary structure provide support, shape, and external protection to vertebrates enzymes, transport proteins, motor proteins, regulatory proteins, immunoglobulins insoluble in water conferred by a high concentration of hydrophobic amino acid residues both in the interior and surface of the protein dense hydrophobic core, -Keratin evolved for strength tough, insoluble protective structures of varying hardness and flexibility hair, wool, nails, claws, quills, hooves, skin right handed helix parallel orientation of the two strands of -keratin helical path of the supertwist is left- handed, opposite in sense to helix cross-linked by disulfide bonds Myoglobin relatively small oxygen-binding protein of muscle cells stores oxygen and facilitates oxygen diffusion a single polypeptide chain of 153 amino acid residues of known sequence and a single iron protoporphyrin (heme) group backbone: eight relatively straight segments of helix (7-23 amino acid residues) interrupted by bends, some of which are turns Collagen evolved to provide strength high tensile strength, without stretch connective tissue such as tendons, cartilage, the organic matrix of bone, and the cornea of the eye helix is left-handed and has three amino acid residues per turn with three chains (not to be confused with helices) supertwisted with each other superhelical twisting is right-handed in collagen, opposite in sense to the left- handed helix of the chains generally a repeating tripeptide unit, Gly XY, where X is often Pro, and Y is often 4- Hyp Pro and 4-Hyp residues permit the sharp twisting of the collagen helix cross-linked by unusual types of covalent bonds involving Lys, HyLys (5- hydroxylysine), or His residues that are present at a few of the X and Y positions in collagens
Silk Fibroin produced by insects and spiders Soft, flexible filaments polypeptide chains are predominantly in the conformation rich in Ala and Gly residues, permitting a close packing of sheets and an interlocking arrangement of R groups stabilized by extensive hydrogen bonding and by the optimization of van der Waals interactions between sheets does not stretch ( conformation is already highly extended) but is flexible (sheets are held together by weak bonds)