Functionally acceptable substitutions in two α-helical regions of λ repressor

Autor:	Robert T. Sauer, John F. Reidharr‐Olson
Rok vydání:	1990
Předmět:	chemistry.chemical_classification Protein family Stereochemistry Repressor Biology Biochemistry DNA-binding protein Amino acid Protein structure chemistry Structural Biology mental disorders Protein folding Molecular Biology Peptide sequence psychological phenomena and processes Neutral mutation
Zdroj:	Proteins: Structure, Function, and Genetics. 7:306-316
ISSN:	1097-0134 0887-3585
DOI:	10.1002/prot.340070403
Popis:	A method of targeted random mutagenesis has been used to investigate the informational content of 25 residue positions in two alpha-helical regions of the N-terminal domain of lambda repressor. Examination of the functionally allowed sequences indicates that there is a wide range in tolerance to amino acid substitution at these positions. At positions that are buried in the structure, there are severe limitations on the number and type of residues allowed. At most surface positions, many different residues and residue types are tolerated. However, at several surface positions there is a strong preference for hydrophilic amino acids, and at one surface position proline is absolutely conserved. The results reveal the high level of degeneracy in the information that specifies a particular protein fold.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::271eb4d488a4fd42a62ac7c8a0e3f17c https://doi.org/10.1002/prot.340070403 Zobrazit plný text záznamu Plný text