ArticleBiophysical journal2001
Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 64 citations in OpenAlex.
- Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy.Molecules (Basel, Switzerland) · 2016Article
- Are current atomistic force fields accurate enough to study proteins in crowded environments?PLoS computational biology · 2014Article
- His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis.Journal of the American Chemical Society · 2012Article
- 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer.Metallomics : integrated biometal science · 2011Article
- Sequential events in the irreversible thermal denaturation of human brain-type creatine kinase by spectroscopic methods.International journal of molecular sciences · 2010Article
- Dissecting the pretransitional conformational changes in aminoacylase I thermal denaturation.Biophysical journal · 2007Article
- Body temperature-related structural transitions of monotremal and human hemoglobin.Biophysical journal · 2006Article
- Cytochrome C interaction with cardiolipin/phosphatidylcholine model membranes: effect of cardiolipin protonation.Biophysical journal · 2006Article
- Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study.Biophysical journal · 2004Article
- Interaction of horse heart and thermus thermophilus type c cytochromes with phospholipid vesicles and hydrophobic surfaces.Biophysical journal · 2004Article
- Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin.Biophysical journal · 2004Article
- Two-dimensional infrared correlation spectroscopy study of sequential events in the heat-induced unfolding and aggregation process of myoglobin.Biophysical journal · 2003Article
- Effect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis.Biophysical journal · 2002Article
- Calcium-dependent conformational rearrangements and protein stability in chicken annexin A5.Biophysical journal · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two-dimensional infrared correlation spectroscopy (2D-IR) was used in this study to investigate the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol. The influence of temperature on the aggregation has been evaluated by monitoring the intensity of a band at 1616 cm(-1), which is characteristic of aggregated proteins, and the 2D-IR analysis has been used to determine the various secondary structure components of cytochrome c involved before and during its aggregation. The 2D-IR correlation analysis clearly reveals for the first time that aggregation starts to occur between nearly native proteins, which then unfold, yielding to further aggregation of the protein. Later in the aggregation process, the formation of intermolecular bonds and unfolding of the alpha-helices appear to be simultaneous. These results lead us to propose a two-step aggregation process. Finally, the results obtained during the heating period clearly indicate that before the protein starts to aggregate, there is a loosening of the tertiary structure of cytochrome c, resulting in a decrease of the beta-sheet content and an increase of the amount of beta-turns. This study clearly demonstrates the potential of 2D-IR spectroscopy to investigate the aggregation of proteins and this technique could therefore be applied to other proteins such as those involved in fibrilogenesis.
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