γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation
The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stability of the two, it is more susceptible to chemical denaturation by urea. The lower thermod...
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ftcdlib:oai:escholarship.org:ark:/13030/qt3h75g84j 2023-09-05T13:12:24+02:00 γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation Kingsley, Carolyn N Bierma, Jan C Pham, Vyvy Martin, Rachel W 13544 - 13553 2014-11-26 application/pdf https://escholarship.org/uc/item/3h75g84j unknown eScholarship, University of California qt3h75g84j https://escholarship.org/uc/item/3h75g84j public The Journal of Physical Chemistry B, vol 118, iss 47 Eye Disease and Disorders of Vision Animals Catfishes Circular Dichroism Escherichia coli Fish Proteins Humans Models Molecular Nuclear Magnetic Resonance Biomolecular Perciformes Protein Denaturation Protein Stability Protein Structure Secondary Scattering Radiation Sequence Homology Sharks Spectrometry Fluorescence Temperature Urea Zebrafish gamma-Crystallins Physical Sciences Chemical Sciences Engineering article 2014 ftcdlib 2023-08-21T18:05:14Z The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stability of the two, it is more susceptible to chemical denaturation by urea. The lower thermodynamic stability of both toothfish crystallins relative to human γS-crystallin is consistent with the current picture of how proteins from organisms endemic to perennially cold environments have achieved low-temperature functionality via greater structural flexibility. In some respects, the sequences of γS1- and γS2-crystallin are typical of psychrophilic proteins; however, their amino acid compositions also reflect their selection for a high refractive index increment. Like their counterparts in the human lens and those of mesophilic fish, both toothfish crystallins are relatively enriched in aromatic residues and methionine and exiguous in aliphatic residues. The sometimes contradictory requirements of selection for cold tolerance and high refractive index make the toothfish crystallins an excellent model system for further investigation of the biophysical properties of structural proteins. Article in Journal/Newspaper Antarc* Antarctic Antarctic Toothfish University of California: eScholarship Antarctic The Antarctic |
institution |
Open Polar |
collection |
University of California: eScholarship |
op_collection_id |
ftcdlib |
language |
unknown |
topic |
Eye Disease and Disorders of Vision Animals Catfishes Circular Dichroism Escherichia coli Fish Proteins Humans Models Molecular Nuclear Magnetic Resonance Biomolecular Perciformes Protein Denaturation Protein Stability Protein Structure Secondary Scattering Radiation Sequence Homology Sharks Spectrometry Fluorescence Temperature Urea Zebrafish gamma-Crystallins Physical Sciences Chemical Sciences Engineering |
spellingShingle |
Eye Disease and Disorders of Vision Animals Catfishes Circular Dichroism Escherichia coli Fish Proteins Humans Models Molecular Nuclear Magnetic Resonance Biomolecular Perciformes Protein Denaturation Protein Stability Protein Structure Secondary Scattering Radiation Sequence Homology Sharks Spectrometry Fluorescence Temperature Urea Zebrafish gamma-Crystallins Physical Sciences Chemical Sciences Engineering Kingsley, Carolyn N Bierma, Jan C Pham, Vyvy Martin, Rachel W γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation |
topic_facet |
Eye Disease and Disorders of Vision Animals Catfishes Circular Dichroism Escherichia coli Fish Proteins Humans Models Molecular Nuclear Magnetic Resonance Biomolecular Perciformes Protein Denaturation Protein Stability Protein Structure Secondary Scattering Radiation Sequence Homology Sharks Spectrometry Fluorescence Temperature Urea Zebrafish gamma-Crystallins Physical Sciences Chemical Sciences Engineering |
description |
The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stability of the two, it is more susceptible to chemical denaturation by urea. The lower thermodynamic stability of both toothfish crystallins relative to human γS-crystallin is consistent with the current picture of how proteins from organisms endemic to perennially cold environments have achieved low-temperature functionality via greater structural flexibility. In some respects, the sequences of γS1- and γS2-crystallin are typical of psychrophilic proteins; however, their amino acid compositions also reflect their selection for a high refractive index increment. Like their counterparts in the human lens and those of mesophilic fish, both toothfish crystallins are relatively enriched in aromatic residues and methionine and exiguous in aliphatic residues. The sometimes contradictory requirements of selection for cold tolerance and high refractive index make the toothfish crystallins an excellent model system for further investigation of the biophysical properties of structural proteins. |
format |
Article in Journal/Newspaper |
author |
Kingsley, Carolyn N Bierma, Jan C Pham, Vyvy Martin, Rachel W |
author_facet |
Kingsley, Carolyn N Bierma, Jan C Pham, Vyvy Martin, Rachel W |
author_sort |
Kingsley, Carolyn N |
title |
γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation |
title_short |
γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation |
title_full |
γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation |
title_fullStr |
γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation |
title_full_unstemmed |
γS-Crystallin Proteins from the Antarctic Nototheniid Toothfish: A Model System for Investigating Differential Resistance to Chemical and Thermal Denaturation |
title_sort |
γs-crystallin proteins from the antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation |
publisher |
eScholarship, University of California |
publishDate |
2014 |
url |
https://escholarship.org/uc/item/3h75g84j |
op_coverage |
13544 - 13553 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctic Toothfish |
genre_facet |
Antarc* Antarctic Antarctic Toothfish |
op_source |
The Journal of Physical Chemistry B, vol 118, iss 47 |
op_relation |
qt3h75g84j https://escholarship.org/uc/item/3h75g84j |
op_rights |
public |
_version_ |
1776200182383247360 |