Robert T. Sauer

TL;DR: Conservation of these binding domains indicates that the mode of substrate recognition characterized here for ClpX will be a conserved feature among Clp/Hsp100 family members and a distinguishing characteristic between this chaperone family and the Hsp70 chaperones.

TL;DR: It is suggested that it is possible to view the stability effects of mutations in intact proteins in a hierarchical fashion, with the stability of units of secondary structure being distinguishable from the stability from tertiary structure.

TL;DR: This study solves the crystal structure of a variant of lambda repressor, which, despite having three larger core substitutions, is more stable than the wild type and shows how a particular set of core residue identities might be selected not because they provide optimal stability but because they provided sufficient stability in addition to the precise structure required for optimal activity.

TL;DR: Determinants in addition to Gln50 must be involved in establishing the differential binding specificity of the engrailed homeodomain, as the QA50 mutant has only a 2-fold reduced affinity for the TAATTA site and discriminates between theTAATTA and TAATCC sites as well as the wild-type protein.

TL;DR: The nucleotide sequence of the λ cI gene is presented and a single mutation (λcI ind−) prevents this cleavage and inactivation of represser7,8 and is identified as the base change responsible for the ind− phenotype of λRepresser.