ArticleMethods in enzymology2011
Strategies for the thermodynamic characterization of linked binding/local folding reactions within the native state application to the LID domain of adenylate kinase from Escherichia coli.
Article in Methods in enzymology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Statistical Thermodynamics of the Protein Ensemble: Mediating Function and Evolution.Annual review of biophysics · 2025Review
- Allosteric Modulation of Neurotransmitter Transporters as a Therapeutic Strategy.Trends in pharmacological sciences · 2020Review
- Uncoupling the Folding and Binding of an Intrinsically Disordered Protein.Journal of molecular biology · 2018Article
- Article
- Solution NMR Spectroscopy for the Study of Enzyme Allostery.Chemical reviews · 2016Review
- Conformational heterogeneity within the LID domain mediates substrate binding to Escherichia coli adenylate kinase: function follows fluctuations.Topics in current chemistry · 2013Review
- Interplay between allostery and intrinsic disorder in an ensemble.Biochemical Society transactions · 2012Review
- Biomolecular dynamics: order-disorder transitions and energy landscapes.Reports on progress in physics. Physical Society (Great Britain) · 2012Article
- Agonism/antagonism switching in allosteric ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural and energetic basis of allostery.Annual review of biophysics · 2012Review
- The role of protein conformational fluctuations in allostery, function, and evolution.Biophysical chemistry · 2011Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Conformational fluctuations in proteins have emerged as an important aspect of biological function, having been linked to processes ranging from molecular recognition and catalysis to allostery and signal transduction. In spite of the realization of their importance, however, the connections between fluctuations and function have largely been empirical, even when they have been quantitative. Part of the problem in understanding the role of fluctuations in function is the fact that the mere existence of fluctuations complicates the interpretation of classic mutagenesis approaches. Namely, mutagenesis, which is typically targeted to an internal position (to elicit an effect), will change the fluctuations as well as the structure of the native state. Decoupling these effects is essential to an unambiguous understanding of the role of fluctuations in function. Here, we use a mutation strategy that targets surface-exposed sites in flexible parts of the molecule for mutation to glycine. Such mutations leave the ground-state structure unaffected. As a result, we can assess the nature of the fluctuations, develop a quantitative model relating fluctuations to function (in this case, molecular recognition), and unambiguously resolve the probabilities of the fluctuating states. We show that when this approach is applied to Escherichia coli adenylate kinase (AK), unique thermodynamic and structural insights are obtained, even when classic mutagenesis approaches targeted to the same region yield ambiguous results.
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Registered trials
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