ArticleJournal of molecular biology2008
Denaturant-induced expansion and compaction of a multi-domain protein: IgG.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Impact of Urea on Monoclonal Antibodies: Multiple Destabilization and Aggregation Effects for Therapeutic Immunoglobulin G Proteins.ACS omega · 2024Article
- Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form.Nucleic acids research · 2018Article
- Article
- Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Journal of the American Chemical Society · 2016Article
- How force unfolding differs from chemical denaturation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Slow and bimolecular folding of a de novo designed monomeric protein DS119.Biophysical journal · 2013Article
- Simple method to enhance the photostability of the fluorescence reporter R6G for prolonged single-molecule studies.The journal of physical chemistry. A · 2013Article
- Spectroscopic studies of protein folding: linear and nonlinear methods.Protein science : a publication of the Protein Society · 2012Review
- Photoinduced electron transfer and fluorophore motion as a probe of the conformational dynamics of membrane proteins: application to the influenza a M2 proton channel.Langmuir : the ACS journal of surfaces and colloids · 2011Article
- Heterogeneous diffusion of a membrane-bound pHLIP peptide.Biophysical journal · 2010Article
- Diffusion as a probe of the heterogeneity of antimicrobial peptide-membrane interactions.Biochemistry · 2010Article
- Unfolded-state dynamics and structure of protein L characterized by simulation and experiment.Journal of the American Chemical Society · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
It is generally believed that unfolded or denatured proteins show random-coil statistics and hence their radius of gyration simply scales with solvent quality (or concentration of denaturant). Indeed, nearly all proteins studied thus far have been shown to undergo a gradual and continuous expansion with increasing concentration of denaturant. Here, we use fluorescence correlation spectroscopy (FCS) to show that while protein A, a multi-domain and predominantly helical protein, expands gradually and continuously with increasing concentration of guanidine hydrochloride (GdnHCl), the F(ab')2 fragment of goat anti-rabbit antibody IgG, a multi-subunit all beta-sheet protein does not show such continuous expansion behavior. Instead, it first expands and then contracts with increasing concentration of GdnHCl. Even more striking is the fact that the hydrodynamic radius of the most expanded F(ab')2 ensemble, observed at 3-4 M GdnHCl, is approximately 3.6 times that of the native protein. Further FCS measurements involving urea and NaCl show that the unusually expanded F(ab')2 conformations might be due to electrostatic repulsions. Taken together, these results suggest that specific interactions need to be considered while assessing the conformational and statistical properties of unfolded proteins, particularly under conditions of low solvent quality.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.