ArticleBiophysical journal2002
Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Fibrillation/defibrillation of myoglobin decorated with gold nanoparticles probed through nanometal surface energy transfer mechanism.RSC advances · 2026Article
- Many Ways Out: Beyond the Two-State Model of Protein Unfolding.ACS omega · 2026Review
- Radiolysis of myoglobin concentrated gels by protons: specific changes in secondary structure and production of carbon monoxide.Scientific reports · 2024Article
- Biomolecules under Pressure: Phase Diagrams, Volume Changes, and High Pressure Spectroscopic Techniques.International journal of molecular sciences · 2022Review
- Article
- Changes in secondary structure of myofibrillar protein and its relationship with water dynamic changes during storage of battered and deep-fried pork slices.Food science and biotechnology · 2018Article
- Enzymes from piezophiles.Seminars in cell & developmental biology · 2018Review
- Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy.Molecules (Basel, Switzerland) · 2016Article
- Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.Angewandte Chemie (International ed. in English) · 2016Article
- Variation in structure of proteins by adjusting reactive oxygen and nitrogen species generated from dielectric barrier discharge jet.Scientific reports · 2016Article
- Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Predicting protein aggregation during storage in lyophilized solids using solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS).Molecular pharmaceutics · 2014Article
- Article
- Pressure and temperature stability of the main apple allergen Mal d1.European biophysics journal : EBJ · 2011Article
- Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH.Archives of biochemistry and biophysics · 2009Article
- Synthesis of functionalized ZnSe nanoparticles and their applications in the determination of bovine serum albumin.Journal of fluorescence · 2009Article
- Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.Biophysical journal · 2008Article
- Stable misfolded states of human serum albumin revealed by high-pressure infrared spectroscopic studies.European biophysics journal : EBJ · 2008Article
- Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy.Biophysical journal · 2007Article
- High-pressure studies of aggregation of recombinant human interleukin-1 receptor antagonist: thermodynamics, kinetics, and application to accelerated formulation studies.Protein science : a publication of the Protein Society · 2005Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We studied the cold unfolding of myoglobin with Fourier transform infrared spectroscopy and compared it with pressure and heat unfolding. Because protein aggregation is a phenomenon with medical as well as biotechnological implications, we were interested in both the structural changes as well as the aggregation behavior of the respective unfolded states. The cold- and pressure-induced unfolding both yield a partially unfolded state characterized by a persistent amount of secondary structure, in which a stable core of G and H helices is preserved. In this respect the cold- and pressure-unfolded states show a resemblance with an early folding intermediate of myoglobin. In contrast, the heat unfolding results in the formation of the infrared bands typical of intermolecular antiparallel beta-sheet aggregation. This implies a transformation of alpha-helix into intermolecular beta-sheet. H/2H-exchange data suggest that the helices are first unfolded and then form intermolecular beta-sheets. The pressure and cold unfolded states do not give rise to the intermolecular aggregation bands that are typical for the infrared spectra of many heat-unfolded proteins. This suggests that the pathways of the cold and pressure unfolding are substantially different from that of the heat unfolding. After return to ambient conditions the cold- or pressure-treated proteins adopt a partially refolded conformation. This aggregates at a lower temperature (32 degrees C) than the native state (74 degrees C).
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