Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin

L. Smeller, P. Rubens, K. Heremans

Research output: Article

110 Citations (Scopus)

Abstract

This work demonstrates that pressure-induced partially unfolded states play a very important role in the aggregation of proteins. The high-pressure unfolding of horse heart metmyoglobin results in an intermediate form that shows a strong tendency to aggregate after pressure release. These aggregates are similar to those that are usually observed upon temperature denaturation. Infrared spectra in the amide I region indicate the formation of an intermolecular antiparallel β-sheet stabilized by hydrogen bonding. The formation of the aggregates is temperature-dependent. Below 30 °C, no aggregation is taking place as seen from the infrared spectra. At 45 and 60 °C, two types of aggregates are formed: one that can be dissociated by moderate pressures and one that is pressure-insensitive. When precompressed at 5 °C, temperature-induced aggregation takes place at lower temperature (38 °C) than without pressure pretreatment (74 °C).

Original languageEnglish
Pages (from-to)3816-3820
Number of pages5
JournalBiochemistry
Volume38
Issue number12
DOIs
Publication statusPublished - márc. 23 1999

Fingerprint

Pressure effects
Myoglobin
Pressure
Temperature
Agglomeration
Metmyoglobin
Infrared radiation
Denaturation
Hydrogen Bonding
Amides
Horses
Hydrogen bonds
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin. / Smeller, L.; Rubens, P.; Heremans, K.

In: Biochemistry, Vol. 38, No. 12, 23.03.1999, p. 3816-3820.

Research output: Article

Smeller, L. ; Rubens, P. ; Heremans, K. / Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin. In: Biochemistry. 1999 ; Vol. 38, No. 12. pp. 3816-3820.
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