ArticleBiophysical journal2003
Two-dimensional infrared correlation spectroscopy study of sequential events in the heat-induced unfolding and aggregation process of myoglobin.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- Effect of thermal and chemical treatments used for SARS-COV-2 inactivation in the measurement of saliva analytes.Scientific reports · 2022Article
- Are current atomistic force fields accurate enough to study proteins in crowded environments?PLoS computational biology · 2014Article
- Effects of spermine NONOate and ATP on the thermal stability of hemoglobin.BMC biophysics · 2012Article
- Sequential events in the irreversible thermal denaturation of human brain-type creatine kinase by spectroscopic methods.International journal of molecular sciences · 2010Article
- Structural transition temperature of hemoglobins correlates with species' body temperature.European biophysics journal : EBJ · 2007Article
- 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
- Oligomerization and aggregation of bovine pancreatic ribonuclease A: characteristic events observed by FTIR spectroscopy.Biophysical journal · 2006Article
- Coarse-grained strategy for modeling protein stability in concentrated solutions. II: phase behavior.Biophysical journal · 2006Article
- Thermal aggregation of SARS-CoV membrane protein.Journal of virological methods · 2005Article
- Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation.Biophysical journal · 2005Article
- Osmophobic effect of glycerol on irreversible thermal denaturation of rabbit creatine kinase.Biophysical journal · 2004Article
- Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin.Biophysical journal · 2004Article
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6 authors.
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Abstract
Unfolding and aggregation are basic problems in protein science with serious biotechnological and medical implications. Probing the sequential events occurring during the unfolding and aggregation process and the relationship between unfolding and aggregation is of particular interest. In this study, two-dimensional infrared (2D IR) correlation spectroscopy was used to study the sequential events and starting temperature dependence of Myoglobin (Mb) thermal transitions. Though a two-state model could be obtained from traditional 1D IR spectra, subtle noncooperative conformational changes were observed at low temperatures. Formation of aggregation was observed at a temperature (50-58 degrees C) that protein was dominated by native structures and accompanied with unfolding of native helical structures when a traditional thermal denaturation condition was used. The time course NMR study of Mb incubated at 55 degrees C for 45 h confirmed that an irreversible aggregation process existed. Aggregation was also observed before fully unfolding of the Mb native structure when a relative high starting temperature was used. These findings demonstrated that 2D IR correlation spectroscopy is a powerful tool to study protein aggregation and the protein aggregation process observed depends on the different environmental conditions used.
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