Characterization of protein-folding pathways by reduced-space modeling
نویسندگان
چکیده
منابع مشابه
Characterization of protein-folding pathways by reduced-space modeling.
Ab initio simulations of the folding pathways are currently limited to very small proteins. For larger proteins, some approximations or simplifications in protein models need to be introduced. Protein folding and unfolding are among the basic processes in the cell and are very difficult to characterize in detail by experiment or simulation. Chymotrypsin inhibitor 2 (CI2) and barnase are probabl...
متن کاملModeling Protein Folding Pathways
Proteins fold through a series of intermediate states called a pathway. Protein folding pathways have been modeled using either simulations or a heirarchy of statistical models. Here we present a series of related statistical models that attempt to predict early, middle and late intermediates along the folding pathway. Isites motifs are discrete models for folding initiation sites. HMMSTR is a ...
متن کاملCharacterization of protein folding by dominant reaction pathways.
We assess the reliability of the recently developed approach denominated dominant reaction pathways (DRP) by studying the folding of a 16 residue beta-hairpin, within a coarse-grained Go-type model. We show that the DRP predictions are in quantitative agreement with the results of molecular dynamics simulations performed in the same model. On the other hand, in the DRP approach, the computation...
متن کاملPredicting protein folding pathways
A structured folding pathway, which is a time ordered sequence of folding events, plays an important role in the protein folding process and hence, in the conformational search. Pathway prediction, thus gives more insight into the folding process and is a valuable guiding tool to search the conformation space. In this paper, we propose a novel 'unfolding' approach to predict the folding pathway...
متن کاملDisulfide-linked protein folding pathways.
Determining the mechanism by which proteins attain their native structure is an important but difficult problem in basic biology. The study of protein folding is difficult because it involves the identification and characterization of folding intermediates that are only very transiently present. Disulfide bond formation is thermodynamically linked to protein folding. The availability of thiol t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2007
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0702265104