ArticlePloS one2015
Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.
Article in PloS one, 2015. 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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Who cites it
13 citing papers in PubMed, 38 citations in OpenAlex.
- Drug-Induced Conformational Dynamics of P-Glycoprotein Underlies the Transport of Camptothecin Analogs.International journal of molecular sciences · 2023Article
- Role of Plasma Membrane at Dielectric Relaxations and Intermembrane Interaction in Human Erythrocytes.Membranes · 2023Article
- Quantification of Structural Integrity and Stability Using Nanograms of Protein by Flow-Induced Dispersion Analysis.Molecules (Basel, Switzerland) · 2022Article
- Trp Fluorescence Redshift during HDL Apolipoprotein Denaturation Is Increased in Patients with Coronary Syndrome in Acute Phase: A New Assay to Evaluate HDL Stability.International journal of molecular sciences · 2021Article
- Unfolding of Helical Poly(Polymers · 2021Article
- Multiple Functions of Spectrin: Convergent Effects.The Journal of membrane biology · 2020Review
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Ameliorating amyloid aggregation through osmolytes as a probable therapeutic molecule against Alzheimer's disease and type 2 diabetes.RSC advances · 2020Article
- Four Cysteine Residues Contribute to Homodimerization of Chicken Interleukin-2.International journal of molecular sciences · 2019Article
- Anti-band 3 and anti-spectrin antibodies are increased in Plasmodium vivax infection and are associated with anemia.Scientific reports · 2018Article
- Structural, thermodynamic, and phosphatidylinositol 3-phosphate binding properties of Phafin2.Protein science : a publication of the Protein Society · 2017Article
- Fluorescence study of the effect of cholesterol on spectrin-aminophospholipid interactions.European biophysics journal : EBJ · 2015Article
- Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.Journal of fluorescence · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the conformational stability of the two homologous membrane skeletal proteins, the erythroid and non-erythroid spectrins, in their dimeric and tetrameric forms respectively during unfolding in the presence of urea and guanidine hydrochloride (GuHCl). Fluorescence and circular dichroism (CD) spectroscopy have been used to study the changes of intrinsic tryptophan fluorescence, anisotropy, far UV-CD and extrinsic fluorescence of bound 1-anilinonapthalene-8-sulfonic acid (ANS). Chemical unfolding of both proteins were reversible and could be described as a two state transition. The folded erythroid spectrin and non-erythroid spectrin were directly converted to unfolded monomer without formation of any intermediate. Fluorescence quenching, anisotropy, ANS binding and dynamic light scattering data suggest that in presence of low concentrations of the denaturants (up-to 1M) hydrogen bonding network and van der Waals interaction play a role inducing changes in quaternary as well as tertiary structures without complete dissociation of the subunits. This is the first report of two large worm like, multi-domain proteins obeying twofold rule which is commonly found in small globular proteins. The free energy of stabilization (ΔGuH20) for the dimeric spectrin has been 20 kcal/mol lesser than the tetrameric from.
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