Recognition peptide

The understanding of the mechanistic principles underlying the catalytic chemistry of metalloproteases has been applied in the design and synthesis of a number of biomimetic metal complexes that ftinction as artificial proteases. These complexes include mononuclear wateractivating complexes, and multinuclear complexes that combine carboxyl terminal recognition, peptide carbonyl polarization, and water nucleophile activation fimctions. ... 

Neduva, V, Binding, R., Su-Angrand, 1., Stark, A., de Masi, F., Gibson, T.J., Lewis, J., Serrano, L. and Russell, R.B. (2005) Systematic discovery of new recognition peptides mediating protein interaction networks. PLoS Biol. 3, e405. 

Tsigelny, I., Grant, B. D., Taylor, S. S., Ten Eyck, L. F. Catalytic subunit of cAMP-dependent protein kinase Electrostatic features and peptide recognition. Biopolymers 39 (1996) 353-365. 

Meador, W.E., Means, A.R., Quiocho, F.A. Target enzyme recognition by calmodulin 2.4 A stmcture of a calmodulin-peptide complex. Science 257 1251-1255, 1992. 

Fairall, L., et al. The crystal structure of a two zinc finger peptide reveals an extension to the rules for zinc finger/DNA recognition. Nature 366 483-487, 1993. 

EMPl, selected by phage display from random peptide libraries, demonstrates that a dimer of a 20-residue peptide can mimic the function of a monomeric 166-residue protein. In contrast to the minimized Z domain, this selected peptide shares neither the sequence nor the structure of the natural hormone. Thus, there can be a number of ways to solve a molecular recognition problem, and combinatorial methods such as phage display allow us to sort through a multitude of structural scaffolds to discover novel solutions. 

Figure 17.12 Ribbon diagram of EMPl bound to the extracellular domain of the erythropoietin receptor (EBP). Binding of EMPl causes dimerization of erythropoietin receptor. The x-ray crystal structure of the EMPl-EBP complex shows a nearly symmetrical dimer complex in which both peptide monomers interact with both copies of EBP. Recognition between the EMPl peptides and EBP utilizes more than 60% of the EMPl surface and four of six loops in the erythropoietin-binding pocket of EBP.

Investigation of immune recognition segments in presynapsis and postsynapsis neurotoxins (macrocyclic peptides) 98KPS22. 

Petir Victor Edman (1916-1977) was born in Stockholm, Sweden, and received an M.D. in 1946 at the Karolinska Institute. After a year in the United States at the Rockefeller Institute, he returned to Sweden as professor at the University of Lund. In 1957, he moved to St. Vincent s School of Medical Research in Melbourne, Australia, where he developed and automated the method of peptide sequencing that bears his name. A reclusive man, he never received the prizes or recognition merited by the importance or his work. 

Conjugation of DOX with copolymers or peptides Recognition of DOX by tumor-specific receptors or proteases Investigational... 

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