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On the evolutionary conservation of protein dynamics: Comment on “Comparing proteins by their internal dynamics: Exploring structure–function relationships beyond static structural alignments” by Cristian Micheletti
Comment on "Comparing proteins by their internal dynamics: Exploring structure-function relationships beyond static structural alignments" by Cristian Micheletti
Analyzing the effect of homogeneous frustration in protein folding
The energy landscape theory has been an invaluable theoretical framework in the understanding of biological processes such as protein folding, oligomerization, and functional transitions. According to the theory, the energy ...
On the dynamical incompleteness of the Protein Data Bank
(Oxford University Press, 2017-07)
Major scientific challenges that are beyond the capability of individuals need to be addressed by multi-disciplinary and multi-institutional consortia. Examples of these endeavours include the Human Genome Project, and ...
The β-isoform of heat shock protein hsp-90 is structurally related with human microtubule-interacting protein Mip-90
Through major research advances in the study of cytoskeletal organization, an integrated view of the complexity of this system has emerged. Recent findings on the microtubule-interacting protein Mip-90, which associates ...
Mapping eIF5A binding sites for Dys1 and Lia1: In vivo evidence for regulation of eIF5A hypusination
The evolutionarily conserved factor eIF5A is the only protein known to undergo hypusination, a unique posttranslational modification triggered by deoxyhypusine synthase (Dys1). Although eIF5A is essential for cell viability, ...