Keratin extended structure

The Structure of the a-Keratins Was Determined with the Help of Molecular Models The fi-Keratins Form Sheetlike Structures with Extended Polypeptide Chains Collagen Forms a Unique Triple-Stranded Structure Globular Protein Structures Are Extremely Varied and Require a More Sophisticated Form of Analysis Folding of Globular Proteins Reveals a Hierarchy of Structural Organization... 

The fi-Keratins Form Sheetlike Structures with Extended Polypeptide Chains... 

Appendageal structures commonly found within the skin are the hairs, hair follicles, associated sebaceous glands, apocrine and eccrine sweat glands, and arrector pili muscles. Hairs are formed by epidermal invaginations. These keratinized structures traverse the dermis and may extend into the hypodermis. The free part of the hair above the surface of the skin is the hair shaft, and the part deep within the dermis is the hair root, which forms an expanded knob-like structure called the hair bulb. This is composed of a matrix of epithelial cells in different stages of differentiation. Hair is composed of three concentric epithelial cell layers the outermost thin cuticle, a densely packed keratinized cortex, and a central medulla of cuboidal cells. The hair follicle consists of four major components (1) internal root sheath (internal root sheath cuticle, granular layer, pale epithelial layer) (2) external root sheath (several layers similar to the epidermis) (3) dermal papilla (connective tissue) and (4) hair matrix (comparable to the stratum basale of the epidermis). 

The wide angle x-ray diffraction pattern of undeformed corneum exhibits diffuse halos at 4.6 A and 9.8 A common to proteins (Figure 4). The lack of the 5.1-A reflection characteristic of alpha-keratin structures in undeformed comeum suggests that the protein is considerably less oriented and perhaps of a lower alpha content than wool. This is supported by the fact that the 5.1-A reflection begins to appear in samples of comeum which were hydrated and stretched to 100% or more (Figure 6) and allowed to dry in the extended state. The increased orientation of the lipid reflections in the stretched sample demonstrates further their association with the orienting protein fibrils. 

The jS form of keratin requires still additional models. And, continuing the order of decreasing certainty, these models are again less well corroborated by experimental observations than are the a-helix or a-keratin structures. Pauling and Corey (1598) presented the pleated sheets to explain /3-keratins. These sheets are made up of extended peptide chains H bonded essentially side by side. Two are shown in Fig. 10-7. 

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