Fibrous Proteins Globular Proteins

polypeptide chains arranged in long strands or

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)