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Chem. , 85, 2870-2871. H. (1982) Proteins 8, 377-385. Korner, T. W. (1988) Fourier Analysis, Cambridge University Press, Cambridge, UK. M. (1989) Meth. Enzym. 177, 159-204. M. (1996) 1. Magn. Reson. B, 112, 79-81. , and Kestler, H. (1993) Biopolymers 33,1003-1017. M. (1988) Protein Eng. 2, 27-38. Oldfield, E. (1995) J. Biomol. NMR 5, 217-225. A. (1994) 1. Mol. Bioi. 244, 183-197. , and Griesinger, e. (1997) Science 276,1230-1233. Richards, EM. (1997) Annu. Rev. Biophys. Biomo!. Struet. 26, 1-25.

1. General The common requirement of all selection techniques is to provide such a linkage and physically connect the phenotype with the genotype of the protein (Phizicky and Fields, 1995). That is, if a particular protein molecule has more desirable properties than the rest, because it carries one or more useful mutations, there must be a way of amplifying and immortalizing this particular sequence. Hence, one must achieve a I: I physical linkage of the DNA sequence (the genotype, which can be inherited) and the protein sequence (the phenotype, which provides the properties).

Away from the nearest active sites. , 1991). , 1995). Hemoglobin Hemoglobin is the first oligomeric allosteric protein for which the T to R transition was structurally characterized (Perutz, 1989). The quaternary change involves a rotation of 15° of an u]13] dimer relative to the u 213 2 dimer when 02 binds to the heme iron in this tetrameric oligomer. \ in the moveable interface between u 213 2 and u]13] (Perutz, 1989; Baldwin and Chothia, 1979). This shift includes loss of a hydrogen bond between Tyr 42u and Asp 9913 in the T form and a gain of a hydrogen bond between Asp 94u and Asn 10213 in the R form as the helices repack.

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