Structural heterogeneity of the various forms of apomyoglobin

Implications for protein folding

Rudolf Gilmanshin, R. Brian Dyer, Robert Callender

Research output: Contribution to journalArticle

41 Citations (Scopus)

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 significant hydrophobic collapse in the rest of the protein molecule. From the current studies and other results, a rather detailed picture of the folding of myoglobin is presented, on the level of specific structures and their thermodynamical properties as well as formation kinetics.

Original languageEnglish (US)
Pages (from-to)2134-2142
Number of pages9
JournalProtein Science
Volume6
Issue number10
StatePublished - Oct 1997

Fingerprint

Protein folding
Protein Folding
Tryptophan
Denaturation
Temperature
Proteins
Fluorescence
Myoglobin
Conformations
Molten materials
Nucleation
Hot Temperature
Molecules
Kinetics
Acids
apomyoglobin
Monitoring

Keywords

  • Apomyoglobin
  • Denaturation
  • Protein folding
  • Temperature melting
  • Tryptophan fluorescence

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structural heterogeneity of the various forms of apomyoglobin : Implications for protein folding. / Gilmanshin, Rudolf; Dyer, R. Brian; Callender, Robert.

In: Protein Science, Vol. 6, No. 10, 10.1997, p. 2134-2142.

Research output: Contribution to journalArticle

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