Multiple phases of protien gels

Annaka Masahiko; Toyoichi Tanaka

doi:10.1016/0378-4371(94)90416-2

Multiple phases of protien gels

Annaka Masahiko, Toyoichi Tanaka

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

A multiple phase transition was observed in gels made by covalently cross-linking proteins in either native or denatured state. The enzymatic activity of the gels prepared from native α-chymotrypsin was determined for each of the multiple phases. The reversibility of the swelling degrees and the enzymatic reaction rates upon phase transition suggests that the protein is at a free energy minimum and thus in a phase.

Original language	English
Pages (from-to)	40-46
Number of pages	7
Journal	Physica A: Statistical Mechanics and its Applications
Volume	204
Issue number	1-4
DOIs	https://doi.org/10.1016/0378-4371(94)90416-2
Publication status	Published - Mar 1 1994
Externally published	Yes

All Science Journal Classification (ASJC) codes

Statistics and Probability
Condensed Matter Physics

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10.1016/0378-4371(94)90416-2

Cite this

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title = "Multiple phases of protien gels",

abstract = "A multiple phase transition was observed in gels made by covalently cross-linking proteins in either native or denatured state. The enzymatic activity of the gels prepared from native α-chymotrypsin was determined for each of the multiple phases. The reversibility of the swelling degrees and the enzymatic reaction rates upon phase transition suggests that the protein is at a free energy minimum and thus in a phase.",

author = "Annaka Masahiko and Toyoichi Tanaka",

year = "1994",

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doi = "10.1016/0378-4371(94)90416-2",

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AU - Masahiko, Annaka

AU - Tanaka, Toyoichi

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N2 - A multiple phase transition was observed in gels made by covalently cross-linking proteins in either native or denatured state. The enzymatic activity of the gels prepared from native α-chymotrypsin was determined for each of the multiple phases. The reversibility of the swelling degrees and the enzymatic reaction rates upon phase transition suggests that the protein is at a free energy minimum and thus in a phase.

AB - A multiple phase transition was observed in gels made by covalently cross-linking proteins in either native or denatured state. The enzymatic activity of the gels prepared from native α-chymotrypsin was determined for each of the multiple phases. The reversibility of the swelling degrees and the enzymatic reaction rates upon phase transition suggests that the protein is at a free energy minimum and thus in a phase.

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U2 - 10.1016/0378-4371(94)90416-2

DO - 10.1016/0378-4371(94)90416-2

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AN - SCOPUS:43949153399

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JO - Physica A: Statistical Mechanics and its Applications

JF - Physica A: Statistical Mechanics and its Applications

IS - 1-4

ER -

Multiple phases of protien gels

Abstract

All Science Journal Classification (ASJC) codes

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