ArticleBiophysical journal2006
Oligomerization and aggregation of bovine pancreatic ribonuclease A: characteristic events observed by FTIR spectroscopy.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 38 citations in OpenAlex.
- Submolecular Resolution of β‑Sheet Plasticity: Decoding Mutations and PTMs in Protein Aggregation Disorders.ACS central science · 2025Article
- Contributions of the C-terminal domain to poly(A)-specific ribonuclease (PARN) stability and self-association.Biochemistry and biophysics reports · 2019Article
- Differential Scanning Fluorimetry provides high throughput data on silk protein transitions.Scientific reports · 2014Article
- Article
- Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease.International journal of molecular sciences · 2011Review
- Sequential events in the irreversible thermal denaturation of human brain-type creatine kinase by spectroscopic methods.International journal of molecular sciences · 2010Article
- Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.Biophysical journal · 2008Article
- Dissecting the pretransitional conformational changes in aminoacylase I thermal denaturation.Biophysical journal · 2007Article
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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
Nonnative protein aggregation, which is a common feature in biotechnology, is also a clinical feature in more than 20 serious degenerative diseases. We studied the specific events of bovine pancreatic ribonuclease A thermal aggregation by a combination of second derivative infrared analysis and two-dimensional infrared correlation spectroscopy. By comparing the events that occur in reversible and irreversible thermal unfolding processes, certain events that were related to protein aggregation were characterized. Particularly, a band that appeared at high temperatures was assigned to the cross beta-structures in oligomers. The effect of pH, NaCl, and ethanol on ribonuclease A oligomerization as well as further aggregation induced by heat were studied and dissimilar effects of these additives were found. Basic pH and NaCl could accelerate the thermal aggregation but did not affect the formation of oligomers, whereas ethanol could increase both the aggregation rate and the population of oligomers. Our results suggested that the aggregation of RNase A might be initiated by hydrophobic interactions, controlled by oligomerization and mediated by electrostatic interactions. Moreover, the strategy of using second derivative and two-dimensional infrared analysis might provide a potential powerful tool to study the events that are directly related to the initiation of protein aggregation.
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