US PATENT SUBCLASS 530 / 353
.~ Scleroproteins, e.g., fibroin, elastin, silk, etc.

Current as of: June, 1999
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530 /   HD   CHEMISTRY: NATURAL RESINS OR DERIVATIVES; PEPTIDES OR PROTEINS; LIGNINS OR REACTION PRODUCTS THEREOF

350  DF  PROTEINS, I.E., MORE THAN 100 AMINO ACID RESIDUES {14}
353.~ Scleroproteins, e.g., fibroin, elastin, silk, etc. {3}
354  DF  .~.~> Gelatin {1}
356  DF  .~.~> Collagen
357  DF  .~.~> Keratin

DEFINITION

Classification: 530/353

Scleroproteins, e.g., fibroin, elastin, silk, etc.:

(under subclass 350) Proteins having the structure of scleroproteins and compounds derived from these by addition to or deletion of parts of the polypeptide structure.

(1) Note. Physical Properties. Scleroproteins are subdivided on the basis of chain conformation into: A. alpha-helicial structure, e.g., alpha-keratins; B. Beta-pleated sheet structure, e.g., Beta-keratins, silk-fibroin; C. triple helical structure, e.g., collagen. Conformation is related to amino acid composition. The amino acid composition of Scleroproteins with Beta-pleated sheet structure shows 90 percent of the simple amino acids glycine, alanine and serine. Beta-keratin also contains a large number of cystine residues. Collagen characteristically contains high concentration of the nonhelix forming amino acid, proline and hydroxyproline.