FTIR spectroscopy and sequence prediction: Structure of human α[sub 2]-macroglobulin (original) (raw)

1998

Abstract

ABSTRACT The structure of a plasma proteinase inhibitor alpha2-Macroglobulin (alpha2m) is determined by FTIR spectroscopy and a number of sequence-structure prediction algorithms. In addition, alpha2M dimers and complexes with methylamine and trypsin are examined. Our FTIR results estimate a helix content of 5-15% and a beta-sheet content of 28-36%. None of the sequence prediction algorithms used in this study predicted values close to experimental data. Considerable differences in the FTIR spectra of alpha2M dimer are observed and somewhat smaller changes are seen upon reaction of alpha2M with methylamine and dithiodipyridine (DTP).

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