Conformation-Dependent Design of Sequences in Copolymers II
DOI: 10.1007/12_053
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Approaches to Chemical Synthesis of Protein-Like Copolymers

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Cited by 23 publications
(8 citation statements)
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“…Experimental work in this field has been complemented with theoretical predictions. It has been shown that in dilute solution and at low ionic strength the chains self-assemble and adopt a “pearl-necklace” morphology. Intermolecular aggregation has also been experimentally observed. , Copolymers that consist of short sequences of hydrophobic units separated by short sequences of charged hydrophilic units have also been studied as models for proteins. It was shown that with an appropriate arrangement of the hydrophobic and charged sequences the polymer chains collapse into single-chain globules similar to the coil-to-globule transition of proteins.…”
Section: Introductionmentioning
confidence: 99%
“…Experimental work in this field has been complemented with theoretical predictions. It has been shown that in dilute solution and at low ionic strength the chains self-assemble and adopt a “pearl-necklace” morphology. Intermolecular aggregation has also been experimentally observed. , Copolymers that consist of short sequences of hydrophobic units separated by short sequences of charged hydrophilic units have also been studied as models for proteins. It was shown that with an appropriate arrangement of the hydrophobic and charged sequences the polymer chains collapse into single-chain globules similar to the coil-to-globule transition of proteins.…”
Section: Introductionmentioning
confidence: 99%
“…Despite a very broad distribution of block lengths, the polymers obtained via the conformation-dependent sequence design are able to form stable segregated structures. The stability of globules with a hydrophobic core and a polar shell formed by protein-like copolymers was demonstrated in the computer simulations and in the theory [7,8] and also experimentally [9,10].…”
Section: Balls Packed In a Body-centered Cubic Latticementioning
confidence: 95%
“…The choice of these monomers associated with the fact that on their basis amphiphilic synthetic thermoresponsive polymers are able to be produced, [27] including proteinlike polymers, which are perspective enzyme-like catalysts. [28,29] Later, the offered two-dimensional scale of the amphiphilicity was successfully used by Okhapkin and coauthors for the estimation of the properties of amino acid residues of proteins. [30] These experiments confirmed the universality of the method for the evaluation of the amphiphilicity of various organic substances, and confirmed prospects for the offered approach for the understanding of the relation of the composition of natural proteins with their unique thermosensitive properties.…”
Section: Introductionmentioning
confidence: 99%