By Greta Pifat-Mrzljak
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Extra resources for Supramolecular structure and function 8, Volume 8
At the binding site they adopt a geometry that places their peptide bonds in similar orientation even so being reversed in the two cases. The backbone amide 42 Gerhard Klebe Figure 8: a: The orientation of the OH group at C1 of N-acetylglucosamide (15) gives rise to different diastereomers. Due to this difference the recognition properties are substantially modified and binding modes with reversed orientation are observed. Only the amide groups are equivalently recognized by Asn59 and Ala107. The remaining parts of the molecules‚ including the distinct C1 OH group‚ are placed to opposite sides of the binding pocket of lysozyme.
1989, Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin. Biochemistry 28: 1493-1497. 22. Schmid, R. , 1998, Lipases: Interfacial Enzymes with Attractive Applications. Angew. Chem. Int. Ed. 37: 1608-1633 23. Chen, C. , 1989, General Aspects and Optimization of Enantioselective Biocatalysis in Organic Solvents. The Use of Lipases. Angew. Chem. Int. Ed. Engl. 28: 695-708 24. Gutman, A. , 1995, Synthetic Applications of Enzymatic Reactions in Organic Solvents.
J. Protein multiple sequence alignment and flexible pattern matching. Methods Enzymol. 183‚ 403-428. (1990). M. & Park‚ J. Fast assignment of protein structures to sequences using the intermediate sequence library PDB-ISL. 16‚ 117-124 (2000). ‚ Luthy‚ R. & Eisenberg‚ D. A method to identify protein sequences that fold into a known three-dimensional structure. Science 253‚ 164-170 (1991). R. M. A new approach to protein fold recognition. Nature 358‚ 86-89 (1992). J. & Weitckus‚ S. Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of known protein conformations.
Supramolecular structure and function 8, Volume 8 by Greta Pifat-Mrzljak