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Showing 1 to 6 of 6 for “"coupled folding and binding"”.
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Kinetic Characterization of the Coupled Folding and Binding Mechanism of Bacterial RNase P Protein: an Intrinsically Unstructured Protein
<p>Understanding the interconversion between the thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional roles of these states in biological systems. The protein component of …
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Biophysical Studies of Protein Assemblies
… of interatomic interactions results in chain folding, through which proteins may acquire defined structures. This spatial organisation is encoded by the protein sequence itself; the so-called thermodynamic hypothesis formulated by Anfinsen in 1961. A defined structure is often considered a …
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From disorder to order: the importance of context in protein folding and binding mechanisms
… aims to shed light on how context can influence folding and binding mechanisms. First, we used SasG – a bacterial protein that defies the disorder prediction with its unique sequence composition and unusual structure – as a template to investigate co-translational folding, and how the presence of …
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Functional Relevance of Protein Disorder: Why is Disorder Favourable?
… or partly structured upon interaction with their binding partners. This process, known as coupled folding and binding raises the question what comes first – folding of the IDP or binding to its partner protein followed by folding. This thesis focuses on understanding the role of disorder in …
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Probing Order within Intrinsically Disordered Proteins
… Much effort was directed to fully understand the mechanisms behind how and why proteins fold, with natively unfolded proteins thought to be experimental artefacts. Today, the field of natively unfolded – or so-called intrinsically disordered – proteins, is rapidly developing. Protein …
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Elucidating the Structural and Dynamical Properties of the Intrinsically Disordered Protein Nrf2 Using Molecular Dynamics Simulations
… The focus was to uncover the conformational landscape of Nrf2’s Neh4 and Neh5 domains, which participate in crucial interactions for complete transcriptional activation. Since Nrf2 is an intrinsically disordered protein (IDP), molecular dynamics simulations were employed to capture its dynamic …