Results 141 to 150 of about 3,029 (158)
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Buffer-Specific Interactions of Imidazolium with Elastin-Like Polypeptides
The Journal of Physical Chemistry BBuffers are commonly added to protein solutions to stabilize their pH and are typically assumed to not influence any other property of the solution. A series of observations, however, indicate buffer-specific effects on protein stability, suggesting interactions of buffers with proteins.
Julia Keil, Nico F. A. van der Vegt
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Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective
Journal of Chemical Theory and ComputationElastin-like polypeptides (ELPs) are a class of bioengineered polymers that mimic the hydrophobic repeat units of the precursor of the elastin protein. These segments drive self-aggregation, a process influenced by various stimuli such as temperature, pH, salt concentration, hydrophobicity of guest amino acid residues, etc.
Piyali Mukherjee +2 more
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Protease-Driven Phase Separation of Elastin-Like Polypeptides
BiomacromoleculesElastin-like polypeptides (ELPs) are a promising material platform for engineering stimuli-responsive biomaterials, as ELPs undergo phase separation above a tunable transition temperature. ELPs with phase behavior that is isothermally regulated by biological stimuli remain attractive for applications in biological systems.
Brendan M. Wirtz +4 more
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Thermosensitive Vesicles from Chemically Encoded Lipid‐Grafted Elastin‐like Polypeptides
Angewandte Chemie - International Edition, 2021Elisabeth Garanger +2 more
exaly
Fen zi xi bao sheng wu xue bao = Journal of molecular cell biology, 2009
Elastin-like polypeptides (ELPs) are biological macromolecules designed on the elastic structure and composition. ELPs are thermally responsive polypeptides that undergo reversible inverse phase transition. Below their inverse transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, phase transition occurs ...
Fan, Hu +6 more
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Elastin-like polypeptides (ELPs) are biological macromolecules designed on the elastic structure and composition. ELPs are thermally responsive polypeptides that undergo reversible inverse phase transition. Below their inverse transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, phase transition occurs ...
Fan, Hu +6 more
openaire +1 more source
Platelet Adhesion and Fibrinogen Accretion on a Family of Elastin-Like Polypeptides
Journal of Biomaterials Science, Polymer Edition, 2011J P Santerre, J L Brash
exaly