Energy landscapes of functional proteins are inherently risky
نویسندگان
چکیده
منابع مشابه
Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins.
Large-scale motions of biomolecules involve linear elastic deformations along low-frequency normal modes, but for function nonlinearity is essential. In addition, unlike macroscopic machines, biological machines can locally break and then reassemble during function. We present a model for global structural transformations, such as allostery, that involve large-scale motion and possible partial ...
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The understanding of the relation between the amino acid sequence and the spatial structure of the protein is an open task since many decades. Some tools for the prediction of protein structures from known ones were developed, but they let unanswered fundamental questions about properties of folded proteins and the folding process itself. Recently, coarse-grained models were developed, which ar...
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The application of bioinformatics methodologies to proteins inherently lacking 3D structure has brought increased attention to these macromolecules. Here topics concerning these proteins are discussed, including their prediction from amino acid sequence, their enrichment in eukaryotes compared to prokaryotes, their more rapid evolution compared to structured proteins, their organization into sp...
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Are User Runtime Estimates Inherently Inaccurate?
Computer system batch schedulers typically require information from the user upon job submission, including a runtime estimate. Inaccuracy of these runtime estimates, relative to the actual runtime of the job, has been well documented and is a perennial problem mentioned in the job scheduling literature. Typically users provide these estimates under circumstances where their job will be killed ...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2014
ISSN: 1552-4450,1552-4469
DOI: 10.1038/nchembio.1670