On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).
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Comment on "Relating side chain organization of PNIPAm with its conformation in aqueous methanol" by D. Mukherji, M. Wagner, M. D. Watson, S. Winzen, T. E. de Oliveira, C. M. Marques and K. Kremer, Soft Matter, 2016, 12, 7995.Comment on "Thermal compaction of the intrinsically disordered protein tau: entropic, structural, and hydrophobic factors" by A. Battisti, G. Ciasca, A. Grottesi and A. Tenenbaum, Phys. Chem. Chem. Phys., 2017, 19, 8435.Insight into the effect mechanism of urea-induced protein denaturation by dielectric spectroscopy.A driving force for polypeptide and protein collapse.An alternative explanation of the cononsolvency of poly(N-isopropylacrylamide) in water-methanol solutions.Molecular origin of urea driven hydrophobic polymer collapse and unfolding depending on side chain chemistry.New endeavours involving the cooperative behaviour of TMAO and urea towards the globular state of poly(N-isopropylacrylamide)
P2860
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P2860
On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年學術文章
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2016年學術文章
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2016年學術文章
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name
On urea's ability to stabilize the globule state of poly
@nl
On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).
@en
type
label
On urea's ability to stabilize the globule state of poly
@nl
On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).
@en
prefLabel
On urea's ability to stabilize the globule state of poly
@nl
On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).
@en
P2860
P356
P1476
On urea's ability to stabilize the globule state of poly(N-isopropylacrylamide).
@en
P2093
Andrea Pica
Giuseppe Graziano
P2860
P304
14426-14433
P356
10.1039/C5CP07507F
P407
P577
2016-05-12T00:00:00Z