ArticleJournal of molecular biology2008
Thermodynamics, kinetics, and salt dependence of folding of YopM, a large leucine-rich repeat protein.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- How a highly acidic SH3 domain folds in the absence of its charged peptide target.Protein science : a publication of the Protein Society · 2023Article
- A Second Backbone: The Contribution of a Buried Asparagine Ladder to the Global and Local Stability of a Leucine-Rich Repeat Protein.Biochemistry · 2019Article
- High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.Journal of molecular biology · 2018Article
- Electrostatic Interactions and Protein Competition Reveal a Dynamic Surface in Gold Nanoparticle-Protein Adsorption.The journal of physical chemistry. C, Nanomaterials and interfaces · 2016Article
- Distribution and Evolution of Yersinia Leucine-Rich Repeat Proteins.Infection and immunity · 2016Article
- Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.PloS one · 2015Article
- Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment.Protein science : a publication of the Protein Society · 2014Article
- Diffuse transition state structure for the unfolding of a leucine-rich repeat protein.Physical chemistry chemical physics : PCCP · 2014Article
- Crystal structure of an engineered YopM-InlB hybrid protein.BMC structural biology · 2014Article
- Article
- Deletion of internal structured repeats increases the stability of a leucine-rich repeat protein, YopM.Biophysical chemistry · 2011Article
- Using Correlated Monte Carlo Sampling for Efficiently Solving the Linearized Poisson-Boltzmann Equation Over a Broad Range of Salt Concentration.Journal of chemical theory and computation · 2010Article
- C-terminal deletion of leucine-rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein.Protein science : a publication of the Protein Society · 2009Article
- What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding?Physical biology · 2009Article
- Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models.Methods in enzymology · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Small globular proteins have many contacts between residues that are distant in primary sequence. These contacts create a complex network between sequence-distant segments of secondary structure, which may be expected to promote the cooperative folding of globular proteins. Although repeat proteins, which are composed of tandem modular units, lack sequence-distant contacts, several of considerable length have been shown to undergo cooperative two-state folding. To explore the limits of cooperativity in repeat proteins, we have studied the unfolding of YopM, a leucine-rich repeat (LRR) protein of over 400 residues. Despite its large size and modular architecture (15 repeats), YopM equilibrium unfolding is highly cooperative, and shows a very strong dependence on the concentration of urea. In contrast, kinetic studies of YopM folding indicate a mechanism that includes one or more transient intermediates. The urea dependence of the folding and unfolding rates suggests a relatively small transition state ensemble. As with the urea dependence, we have found an extreme dependence of the free energy of unfolding on the concentration of salt. This salt dependence likely results from general screening of a large number of unfavorable columbic interactions in the folded state, rather than from specific cation binding.
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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.