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Comparison of the X-ray structure of baboon α-lactalbumin and the tertiary predicted computer models of human α-lactalbumin

✍ Scribed by Barry Robson; Eric Platt

Publisher: Springer Netherlands
Year: 1990
Tongue: English
Weight: 708 KB
Volume: 4
Category: Article
ISSN: 0920-654X
DOI: 10.1007/bf00117402

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✦ Synopsis

The previously predicted structures of human a-lactalbumin by homology with hen egg white lysozyme by an automatic method, after the alignment stage, are compared to the X-ray determined structure of baboon a-lactalbumin. The root mean square by rotation method (RMSR) deviations for 122 C-a atoms between the two models and the X-ray structure are 2.0 A and 2.3/~. The RMSR deviations for all atoms, except for differences in human and baboon sequences, are 2.8 A and 3.1 A. If the flexible C-terminus (residues 112-122) are removed then these RMSR deviations are reduced to 2.4 A and 2.3 A respectively. These results are consistent with the fact that the RMSR de~,iation between the human and baboon X-ray structures increases from residue 112 onwards and is conformationally flexible.

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