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Structural heterogeneity of the various forms of apomyoglobin; Implications for protein folding by Rudolf Gilmanshin; R. Brian Dyer; Robert H. Callender is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Temperature‐induced denaturation transitions of different structural forms of apomyoglobin were studied monitoring intrinsic tryptophan fluorescence. It was found that the tryptophans are effectively screened from solvent both in native and acid forms throughout most of the temperature range tested. Thus, the tryptophans' surroundings do not show a considerable change in structure where major protein conformational transitions have been found in apomyoglobin using other techniques. At high temperatures and under strong destabilizing conditions, the tryptophans' fluorescence parameters show sigmoidal thermal denaturation. These results, combined with previous studies, show that the structure of this protein is heterogeneous, including native‐like (tightly packed) and molten globule‐like substructures that exhibit conformation (denaturation) transitions under different conditions of pH and temperature (and denaturants). The results suggest that the folding of this protein proceeds via two “nucleation” events whereby native‐like contacts are formed. One of these events, which involves AGH “core” formation, appears to occur very early in the folding process, even before sig

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Author

Rudolf Gilmanshin; R. Brian Dyer; Robert H. Callender

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)