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 2023-05-15T14:02:50+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 2014-11-18 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 Animals Catfishes Zebrafish Sharks Perciformes Humans Escherichia coli Urea gamma-Crystallins Fish Proteins Spectrometry Fluorescence Circular Dichroism Nuclear Magnetic Resonance Biomolecular Temperature Protein Structure Secondary Protein Denaturation Sequence Homology Scattering Radiation Models Molecular Protein Stability Chemical Sciences Engineering Physical Sciences article 2014 ftcdlib 2020-01-24T23:56:01Z 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 |
Animals Catfishes Zebrafish Sharks Perciformes Humans Escherichia coli Urea gamma-Crystallins Fish Proteins Spectrometry Fluorescence Circular Dichroism Nuclear Magnetic Resonance Biomolecular Temperature Protein Structure Secondary Protein Denaturation Sequence Homology Scattering Radiation Models Molecular Protein Stability Chemical Sciences Engineering Physical Sciences |
spellingShingle |
Animals Catfishes Zebrafish Sharks Perciformes Humans Escherichia coli Urea gamma-Crystallins Fish Proteins Spectrometry Fluorescence Circular Dichroism Nuclear Magnetic Resonance Biomolecular Temperature Protein Structure Secondary Protein Denaturation Sequence Homology Scattering Radiation Models Molecular Protein Stability Chemical Sciences Engineering Physical Sciences 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 |
Animals Catfishes Zebrafish Sharks Perciformes Humans Escherichia coli Urea gamma-Crystallins Fish Proteins Spectrometry Fluorescence Circular Dichroism Nuclear Magnetic Resonance Biomolecular Temperature Protein Structure Secondary Protein Denaturation Sequence Homology Scattering Radiation Models Molecular Protein Stability Chemical Sciences Engineering Physical Sciences |
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_ |
1766273245785358336 |