Publication
The assembly of helical and b-sheet peptide blocks contg. reactive chain ends results in highly branched chain architectures ("locked-in folds") mimicking native tertiary structures. This mol. kit strategy allows to bypass the protein folding problem in protein de novo design and gives access to protein mimetics of high thermo-dynamic stability. The validity of this concept is exemplified for the design and synthesis of locked-in folds mimicking the zinc finger and MHC folding motifs. [on SciFinder (R)]
Bruno Emanuel Ferreira De Sousa Correia, Casper Alexander Goverde
Bruno Emanuel Ferreira De Sousa Correia, Michael Bronstein, Hamed Khakzad, Casper Alexander Goverde, Arne Schneuing, Ilia Igashov
Bruno Emanuel Ferreira De Sousa Correia, Hamed Khakzad, Casper Alexander Goverde, Stéphane Rosset, Benedict Dieter Gregor Wolf