Synthesis of a genetically engineered repetitive polypeptide containing periodic selenomethionine residues
- Univ. of Massachusetts, Amherst (United States)
Genetically engineered proteins will play an important role in materials science. Many natural proteins have excellent materials properties such as the silks, elastin, and collagen, and, in principle, both these and entirely new protein materials can be produced from artificial genes. Good early progress has been made in this direction, including the synthesis of repetitive proteins predicted to self-assemble into solid lamellae of defined thickness and surface function. While biological synthesis offers the materials scientist superior control over polymer chain architecture, including purity of sequence, size, and stereochemistry, its versatility is limited to the 20 amino acids that can be utilized in protein biosynthesis. First efforts in this direction would logically start with amino acid analogs known to be incorporated during translation. The authors describe here the first genetic synthesis of a periodic protein material in which an amino acid analog, selenomethionine, completely replaces a natural amino acid.
- OSTI ID:
- 6774761
- Journal Information:
- Macromolecules; (United States), Vol. 26:7; ISSN 0024-9297
- Country of Publication:
- United States
- Language:
- English
Similar Records
Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems
Aza-proline effectively mimics L-proline stereochemistry in triple helical collagen
Related Subjects
36 MATERIALS SCIENCE
POLYPEPTIDES
GENETIC ENGINEERING
AMINO ACIDS
BIOSYNTHESIS
MECHANICAL PROPERTIES
METALLOTHIONEIN
STEREOCHEMISTRY
BIOTECHNOLOGY
CARBOXYLIC ACIDS
METALLOPROTEINS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PEPTIDES
PROTEINS
SYNTHESIS
550200* - Biochemistry
360603 - Materials- Properties