NDLI: Characterization of the folding landscape of monomeric lactose repressor: Quantitative comparison of theory and experiment

Content Provider	PubMed Central
Author	Das, Payel Wilson, Corey J. Fossati, Giovanni Wittung-stafshede, Pernilla Matthews, Kathleen S. Clementi, Cecilia
Copyright Year	2005
Abstract	Recent theoretical/computational studies based on simplified protein models and experimental investigation have suggested that the native structure of a protein plays a primary role in determining the folding rate and mechanism of relatively small single-domain proteins. Here, we extend the study of the relationship between protein topology and folding mechanism to a larger protein with complex topology, by analyzing the folding process of monomeric lactose repressor (MLAc) computationally by using a Gō-like Cα model. Next, we combine simulation and experimental results (see companion article in this issue) to achieve a comprehensive assessment of the folding landscape of this protein. Remarkably, simulated kinetic and equilibrium analyses show an excellent quantitative agreement with the experimental folding data of this study. The results of this comparison show that a simplified, completely unfrustrated Cα model correctly reproduces the complex folding features of a large multidomain protein with complex topology. The success of this effort underlines the importance of synergistic experimental/theoretical approaches to achieve a broader understanding of the folding landscape.
Related Links	http://dx.doi.org/10.1073/pnas.0505844102
Ending Page	14574
Page Count	6
Starting Page	14569
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	41
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-10-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment.

The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates

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The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates.

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Characterization of the folding landscape of monomeric lactose repressor: Quantitative comparison of theory and experiment

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Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment.

The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates

Submillisecond folding of monomeric lambda repressor.

The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates.

Minimal length of the lactose operator sequence for the specific recognition by the lactose repressor.

Meeting halfway on the bridge between protein folding theory and experiment

Disordered to ordered folding in the regulation of diphtheria toxin repressor activity

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Characterization of the folding landscape of monomeric lactose repressor: Quantitative comparison of theory and experiment