Literature DB >> 23860838

Effects of a type I antifreeze protein (AFP) on the melting of frozen AFP and AFP+solute aqueous solutions studied by NMR microimaging experiment.

Yong Ba1, Yougang Mao, Luiz Galdino, Zorigoo Günsen.   

Abstract

The effects of a type I AFP on the bulk melting of frozen AFP solutions and frozen AFP+solute solutions were studied through an NMR microimaging experiment. The solutes studied include sodium chloride and glucose and the amino acids alanine, threonine, arginine, and aspartic acid. We found that the AFP is able to induce the bulk melting of the frozen AFP solutions at temperatures lower than 0 °C and can also keep the ice melted at higher temperatures in the AFP+solute solutions than those in the corresponding solute solutions. The latter shows that the ice phases were in super-heated states in the frozen AFP+solute solutions. We have tried to understand the first experimental phenomenon via the recent theoretical prediction that type I AFP can induce the local melting of ice upon adsorption to ice surfaces. The latter experimental phenomenon was explained with the hypothesis that the adsorption of AFP to ice surfaces introduces a less hydrophilic water-AFP-ice interfacial region, which repels the ionic/hydrophilic solutes. Thus, this interfacial region formed an intermediate chemical potential layer between the water phase and the ice phase, which prevented the transfer of water from the ice phase to the water phase. We have also attempted to understand the significance of the observed melting phenomena to the survival of organisms that express AFPs over cold winters.

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Year:  2012        PMID: 23860838      PMCID: PMC3532670          DOI: 10.1007/s10867-012-9291-7

Source DB:  PubMed          Journal:  J Biol Phys        ISSN: 0092-0606            Impact factor:   1.365


  31 in total

1.  Antifreeze Proteins: Structures and Mechanisms of Function.

Authors:  Yin Yeh; Robert E. Feeney
Journal:  Chem Rev       Date:  1996-03-28       Impact factor: 60.622

2.  Antifreeze proteins in Alaskan insects and spiders.

Authors:  J G Duman; V Bennett; T Sformo; R Hochstrasser; B M Barnes
Journal:  J Insect Physiol       Date:  2004-04       Impact factor: 2.354

3.  Superheating of ice crystals in antifreeze protein solutions.

Authors:  Yeliz Celik; Laurie A Graham; Yee-Foong Mok; Maya Bar; Peter L Davies; Ido Braslavsky
Journal:  Proc Natl Acad Sci U S A       Date:  2010-03-09       Impact factor: 11.205

4.  Binding of an oligopeptide to a specific plane of ice.

Authors:  M E Houston; H Chao; R S Hodges; B D Sykes; C M Kay; F D Sönnichsen; M C Loewen; P L Davies
Journal:  J Biol Chem       Date:  1998-05-08       Impact factor: 5.157

5.  Hyperactive antifreeze protein from beetles.

Authors:  L A Graham; Y C Liou; V K Walker; P L Davies
Journal:  Nature       Date:  1997-08-21       Impact factor: 49.962

6.  A biological antifreeze.

Authors:  R E Feeney
Journal:  Am Sci       Date:  1974 Nov-Dec       Impact factor: 0.548

7.  Ice-binding structure and mechanism of an antifreeze protein from winter flounder.

Authors:  F Sicheri; D S Yang
Journal:  Nature       Date:  1995-06-01       Impact factor: 49.962

8.  Fish antifreeze protein and the freezing and recrystallization of ice.

Authors:  C A Knight; A L DeVries; L D Oolman
Journal:  Nature       Date:  1984 Mar 15-21       Impact factor: 49.962

9.  Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via ¹³C-¹⁵N dynamic REDOR NMR.

Authors:  Yougang Mao; Myongho Jeong; Tieli Wang; Yong Ba
Journal:  Solid State Nucl Magn Reson       Date:  2011-03-23       Impact factor: 2.293

10.  Structure determination of a lone alpha-helical antifreeze protein from winter flounder.

Authors:  F Sicheri; D S Yang
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1996-05-01
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  1 in total

1.  Mechanisms of antifreeze proteins investigated via the site-directed spin labeling technique.

Authors:  Antonia Flores; Justin C Quon; Adiel F Perez; Yong Ba
Journal:  Eur Biophys J       Date:  2018-02-27       Impact factor: 1.733

  1 in total

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