L
Laura S. Itzhaki
Researcher at University of Cambridge
Publications - 124
Citations - 5202
Laura S. Itzhaki is an academic researcher from University of Cambridge. The author has contributed to research in topics: Protein folding & Protein structure. The author has an hindex of 38, co-authored 112 publications receiving 4860 citations. Previous affiliations of Laura S. Itzhaki include Medical Research Council.
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The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding
TL;DR: It is suggested that the mechanism of folding ofCI2 may be a common theme in protein folding whereby fundamental folding units of larger proteins, which are modelled by the folding of CI2, form by nucleation-condensation events and coalesce, perhaps in a hierarchical manner.
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The unfolding story of three-dimensional domain swapping.
TL;DR: Experimental studies carried out within the last few years are highlighted that have led to a much greater understanding of the mechanism of domain swapping and of the residue- and structure-specific features that facilitate the process.
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Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
TL;DR: The main transition state for the folding of barnase has some fully formed secondary and tertiary structural elements in the major transition state, and barnase appears to form by a framework process, however, the fully formed framework may be preceded by a global collapse, and a unified folding scheme is presented.
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Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
TL;DR: This work shows that suc1 has two native states, a monomer and a domain-swapped dimer, and shows that their folding pathways are connected by the denatured state, which introduces a kinetic barrier between monomers and dimer under native conditions.
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Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
TL;DR: The kinetics rule out those mechanisms that involve a mixture of fully formed or fully unfolded structures for regions of the barley chymotrypsin inhibitor 2 and barnase, and so those regions are genuinely only partially folded in the transition state.