Format

Send to

Choose Destination
See comment in PubMed Commons below
Proteins. 1990;7(4):306-16.

Functionally acceptable substitutions in two alpha-helical regions of lambda repressor.

Author information

1
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Abstract

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.

PMID:
2199970
DOI:
10.1002/prot.340070403
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center