Cunning simplicity of protein folding landscapes
نویسندگان
چکیده
منابع مشابه
Exploring energy landscapes of protein folding and aggregation.
Human diseases, such as Alzheimer's and Creutzfeldt-Jakob's are associated with misfolding and aggregation of specific proteins into amyloid fibrils sharing a generic cross-beta structure. The self-assembly process is complex, but once a nucleus is formed, rapid fibril formation occurs. Insight into the structures of the oligomers during the lag phase, varying between hours and days, is very di...
متن کاملTheoretical and Computational Studies of Protein Folding Energy Landscapes
Dissertation zur Erlangung der naturwissenschaftlichen Doktorwürde Φ−value analysis by molecular dynamics simulations of reversible folding Replica exchange molecular dynamics simulations of reversible folding F. Rao and A. Caflisch Replica exchange molecular dynamics simulations of amyloid peptide aggregation Summary The present thesis is concerned with the development and application of three...
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Using a statistical mechanical treatment, we study RNA folding energy landscapes. We first validate the theory by showing that, for the RNA molecules we tested having only secondary structures, this treatment (i) predicts about the same native structures as the Zuker method, and (ii) qualitatively predicts the melting curve peaks and shoulders seen in experiments. We then predict thermodynamic ...
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59 KEY TO ABSTRACT NUMBERING
متن کاملConnecting thermal and mechanical protein (un)folding landscapes.
Molecular dynamics simulations supplement single-molecule pulling experiments by providing the possibility of examining the full free energy landscape using many coordinates. Here, we use an all-atom structure-based model to study the force and temperature dependence of the unfolding of the protein filamin by applying force at both termini. The unfolding time-force relation τ(F) indicates that ...
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 2001
ISSN: 1741-0134,1741-0126
DOI: 10.1093/protein/14.8.521