In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 98, No. 4 ( 2001-02-13), p. 1410-1415
Kurzfassung:
An additivity-based sequence to reactivity algorithm for the
interaction of members of the Kazal family of protein inhibitors with six selected serine proteinases is described. Ten consensus variable
contact positions in the inhibitor were identified, and the 19 possible variants at each of these positions were expressed. The free energies
of interaction of these variants and the wild type were measured. For an additive system, this data set allows for the calculation of all
possible sequences, subject to some restrictions. The algorithm was extensively tested. It is exceptionally fast so that all possible
sequences can be predicted. The strongest, the most specific possible, and the least specific inhibitors were designed, and an evolutionary
problem was solved.
Materialart:
Online-Ressource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.98.4.1410
Sprache:
Englisch
Verlag:
Proceedings of the National Academy of Sciences
Publikationsdatum:
2001
ZDB Id:
209104-5
ZDB Id:
1461794-8
SSG:
11
SSG:
12
