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Comparing proteins by their internal dynamics: Exploring structure–function relationships beyond static structural alignments
C Micheletti - Physics of life reviews, 2013 - Elsevier
The growing interest for comparing protein internal dynamics owes much to the realisation
that protein function can be accompanied or assisted by structural fluctuations and …
that protein function can be accompanied or assisted by structural fluctuations and …
Evolutionary biochemistry: revealing the historical and physical causes of protein properties
The repertoire of proteins and nucleic acids in the living world is determined by evolution;
their properties are determined by the laws of physics and chemistry. Explanations of these …
their properties are determined by the laws of physics and chemistry. Explanations of these …
Biophysics of protein evolution and evolutionary protein biophysics
The study of molecular evolution at the level of protein-coding genes often entails comparing
large datasets of sequences to infer their evolutionary relationships. Despite the importance …
large datasets of sequences to infer their evolutionary relationships. Despite the importance …
Structural and functional constraints in the evolution of protein families
High-throughput genomic sequencing has focused attention on understanding differences
between species and between individuals. When this genetic variation affects protein …
between species and between individuals. When this genetic variation affects protein …
Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection
The energy landscape used by nature over evolutionary timescales to select protein
sequences is essentially the same as the one that folds these sequences into functioning …
sequences is essentially the same as the one that folds these sequences into functioning …
Protein folding in the cell: challenges and progress
A Gershenson, LM Gierasch - Current opinion in structural biology, 2011 - Elsevier
It is hard to imagine a more extreme contrast than that between the dilute solutions used for
in vitro studies of protein folding and the crowded, compartmentalized, sticky, spatially …
in vitro studies of protein folding and the crowded, compartmentalized, sticky, spatially …
Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions
The self-assembly of proteins and peptides into polymeric amyloid fibrils is a process that
has important implications ranging from the understanding of protein misfolding disorders to …
has important implications ranging from the understanding of protein misfolding disorders to …
It is widely assumed that new proteins are created by duplication, fusion, or fission of
existing coding sequences. Another mechanism of protein birth is provided by overlap** …
existing coding sequences. Another mechanism of protein birth is provided by overlap** …
Protein thermostability is owing to their preferences to non-polar smaller volume amino acids, variations in residual physico-chemical properties and more salt-bridges
AS Panja, B Bandopadhyay, S Maiti - PloS one, 2015 - journals.plos.org
Introduction Protein thermostability is an important field for its evolutionary perspective of
mesophilic versus thermophilic relationship and for its industrial/therapeutic applications …
mesophilic versus thermophilic relationship and for its industrial/therapeutic applications …
[HTML][HTML] Tuning transcriptional regulation through signaling: a predictive theory of allosteric induction
Allosteric regulation is found across all domains of life, yet we still lack simple, predictive
theories that directly link the experimentally tunable parameters of a system to its input …
theories that directly link the experimentally tunable parameters of a system to its input …