Probing protein stability and proteolytic resistance by loop scanning: a comprehensive mutational analysis.

ABSTRACT: Improvement in protein thermostability was often found to be associated with increase in its proteolytic resistance as revealed by comparative studies of homologous proteins from extremophiles or mutational studies. Structural elements of protein responsible for this association are not firmly established although loops are implicated indirectly due to their structural role in protein stability. To get a better insight, a detailed study of protein wide mutants and their influence on stability and proteolytic resistance would be helpful. To generate such a data set, a model protein, Bacillus subtilis lipase was subjected to loop scanning site-saturation mutagenesis on 86 positions spanning all loops including termini. Upon screening of ~16,000 clones, 17 single mutants with improved thermos

SUBMITTER: Ahmad S 

PROVIDER: S-EPMC3375443 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature