ArticleBiophysical journal2006
Complex folding kinetics of a multidomain protein.
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 25 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 60 citations in OpenAlex.
- Dissecting the Structural Features of Folding Asymmetry and Transient Misfolding in a Multidomain PDZ Scaffold.Small science · 2026Article
- Folding and Binding Kinetics of the Tandem of SH2 Domains from SHP2.International journal of molecular sciences · 2024Article
- Cryptic binding properties of a transient folding intermediate in a PDZ tandem repeat.Protein science : a publication of the Protein Society · 2022Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
- Large Multidomain Protein NMR: HIV-1 Reverse Transcriptase Precursor in Solution.International journal of molecular sciences · 2020Review
- Investigating the trade-off between folding and function in a multidomain Y-family DNA polymerase.eLife · 2020Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- AnThe Journal of biological chemistry · 2017Article
- Article
- Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.PloS one · 2015Article
- Understanding pathogenic single-nucleotide polymorphisms in multidomain proteins--studies of isolated domains are not enough.The FEBS journal · 2013Article
- Thermal stability of chicken brain α-spectrin repeat 17: a spectroscopic study.Journal of biomolecular NMR · 2012Article
- Two immunoglobulin tandem proteins with a linking β-strand reveal unexpected differences in cooperativity and folding pathways.Journal of molecular biology · 2012Article
- Structural basis for the stability of a thermophilic methionine adenosyltransferase against guanidinium chloride.Amino acids · 2012Article
- Monitoring local unfolding of bovine serum albumin during denaturation using steady-state and time-resolved fluorescence spectroscopy.Journal of fluorescence · 2010Article
- Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states.Biophysical chemistry · 2009Article
- Studying the folding of multidomain proteins.HFSP journal · 2008Article
- Cooperativity, connectivity, and folding pathways of multidomain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain.Journal of molecular biology · 2008Article
- Spectrin folding versus unfolding reactions and RBC membrane stiffness.Biophysical journal · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spectrin domains are three-helix bundles, commonly found in large tandem arrays. Equilibrium studies have shown that spectrin domains are significantly stabilized by their neighbors. In this work we show that domain:domain interactions can also have profound effects on their kinetic behavior. We have studied the folding of a tandem pair of spectrin domains (R1617) using a combination of single- and double-jump stopped flow experiments (monitoring folding by both circular dichroism and fluorescence). Mutant proteins were also used to investigate the complex folding kinetics. We find that, although the domains fold and unfold individually, there is a single rate-determining step for both folding and unfolding of the protein. This is consistent with the equilibrium observation of cooperative folding of the entire two-domain protein. The results may have important biological implications. Not only will the protein fold more efficiently during cotranslational folding, but the ability of the multidomain protein to withstand thermal unfolding in the cell will be dramatically increased. This study suggests that caution has to be exercised when extrapolating from single domains to larger proteins with a number of independently folding modules arranged in tandem. The multidomain protein spectrin is certainly more than "the sum of its parts".
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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.