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Evolution and disorder
The evolution of disordered proteins or regions of proteins differs from that of ordered
proteins because of the differences in their sequence composition, intramolecular contacts …
proteins because of the differences in their sequence composition, intramolecular contacts …
From Water and Ions to Crowded Biomacromolecules: In Vivo Structuring of a Prokaryotic Cell
J Spitzer - Microbiology and molecular biology reviews, 2011 - journals.asm.org
The interactions and processes which structure prokaryotic cytoplasm (water, ions,
metabolites, and biomacromolecules) and ensure the fidelity of the cell cycle are reviewed …
metabolites, and biomacromolecules) and ensure the fidelity of the cell cycle are reviewed …
Exploration of biarsenical chemistry—challenges in protein research
The fluorescent modification of proteins (with genetically encoded low‐molecular‐mass
fluorophores, affinity probes, or other chemically active species) is extraordinarily useful for …
fluorophores, affinity probes, or other chemically active species) is extraordinarily useful for …
Structural divergence is more extensive than sequence divergence for a family of intrinsically disordered proteins
The p53 transactivation domain (p53TAD) is an intrinsically disordered protein (IDP) domain
that undergoes coupled folding and binding when interacting with partner proteins like the …
that undergoes coupled folding and binding when interacting with partner proteins like the …
The ionic liquid [C 4 mpy][Tf 2 N] induces bound-like structure in the intrinsically disordered protein FlgM
The A. aeolicus intrinsically disordered protein FlgM has four well-defined α-helices when
bound to σ28, but in water FlgM undergoes a change in tertiary structure. In this work, we …
bound to σ28, but in water FlgM undergoes a change in tertiary structure. In this work, we …
The role of semidisorder in temperature adaptation of bacterial FlgM proteins
Probabilities of disorder for FlgM proteins of 39 species whose optimal growth temperature
ranges from 273 K (0° C) to 368 K (95° C) were predicted by a newly developed method …
ranges from 273 K (0° C) to 368 K (95° C) were predicted by a newly developed method …
FlgM proteins from different bacteria exhibit different structural characteristics
Intrinsically disordered proteins (IDPs) are a unique class of proteins that do not require a
stable structure for function. The importance of IDPs in many biological processes has been …
stable structure for function. The importance of IDPs in many biological processes has been …
Conformational Change Characteristics in the Intrinsically Disordered FlgM Protein from a Hyperthermophile at Two Different Temperatures
YF ZHU, ZX CAO, LL ZHAO… - Acta Physico-Chimica …, 2015 - ingentaconnect.com
The aim of this work was to compare the structural characteristics of the FlgM protein from
the thermophile aquifex aeolicus at room temperature (293 K) and at the physiological …
the thermophile aquifex aeolicus at room temperature (293 K) and at the physiological …
[PDF][PDF] Cold Adaptation of Intrinsically Disordered Structure Studied in p53 Homologs
EC Tilton - 2016 - digital.library.txstate.edu
Structural descriptions of functional biology, commonly known as the protein structure-
function paradigm, state that protein function is dependent upon its well defined three …
function paradigm, state that protein function is dependent upon its well defined three …
Influence of environment and temperature on the structure of the thermophilic intrinsically disordered protein FlgM
EE Carter - 2016 - search.proquest.com
Recently, there has been significant interest in intrinsically disordered proteins (IDPs)
because they challenge the postulate that the structure of a protein dictates its function …
because they challenge the postulate that the structure of a protein dictates its function …