The fi-Keratins Form Sheetlike Structures with Extended Polypeptide Chains

The fi-Keratins Form Sheetlike Structures with Extended Polypeptide Chains 

Two forms of the /3-sheet structure (a) the antiparallel and (b) the parallel fi sheet. The advance per two amino acid residues is indicated for each structure. 

The antiparallel jS sheet. This structure is composed of two or more polypeptide chains in the fully extended form, with hydrogen bonds formed between the chains. Hydrogen bonds are shown as dashed lines. (Illustration copyright by Irving Geis. Reprinted by permission.) 

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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... 

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