Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality
Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No si...
Ausführliche Beschreibung
Gespeichert in:
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Socorro, J. M. [verfasserIn] |
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E-Artikel |
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Englisch |
| Erschienen: |
2000 |
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© Plenum Publishing Corporation 2000 |
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| Übergeordnetes Werk: |
Enthalten in: The protein journal - Dordrecht : Springer Science + Business Media B.V., 2004, 19(2000), 3 vom: 01. Apr., Seite 199-208 |
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| Übergeordnetes Werk: |
volume:19 ; year:2000 ; number:3 ; day:01 ; month:04 ; pages:199-208 |
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10.1023/A:1007055719926 |
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| 520 | |a Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. | ||
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10.1023/A:1007055719926 doi (DE-627)SPR052715140 (SPR)A:1007055719926-e DE-627 ger DE-627 rakwb eng Socorro, J. M. verfasserin aut Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 2000 Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. Olmo, R. aut Teijón, C. aut Blanco, M. D. aut Teijón, J. M. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 19(2000), 3 vom: 01. Apr., Seite 199-208 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:19 year:2000 number:3 day:01 month:04 pages:199-208 https://dx.doi.org/10.1023/A:1007055719926 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_120 GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 19 2000 3 01 04 199-208 |
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10.1023/A:1007055719926 doi (DE-627)SPR052715140 (SPR)A:1007055719926-e DE-627 ger DE-627 rakwb eng Socorro, J. M. verfasserin aut Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 2000 Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. Olmo, R. aut Teijón, C. aut Blanco, M. D. aut Teijón, J. M. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 19(2000), 3 vom: 01. Apr., Seite 199-208 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:19 year:2000 number:3 day:01 month:04 pages:199-208 https://dx.doi.org/10.1023/A:1007055719926 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_120 GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 19 2000 3 01 04 199-208 |
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10.1023/A:1007055719926 doi (DE-627)SPR052715140 (SPR)A:1007055719926-e DE-627 ger DE-627 rakwb eng Socorro, J. M. verfasserin aut Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 2000 Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. Olmo, R. aut Teijón, C. aut Blanco, M. D. aut Teijón, J. M. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 19(2000), 3 vom: 01. Apr., Seite 199-208 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:19 year:2000 number:3 day:01 month:04 pages:199-208 https://dx.doi.org/10.1023/A:1007055719926 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_120 GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 19 2000 3 01 04 199-208 |
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10.1023/A:1007055719926 doi (DE-627)SPR052715140 (SPR)A:1007055719926-e DE-627 ger DE-627 rakwb eng Socorro, J. M. verfasserin aut Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 2000 Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. Olmo, R. aut Teijón, C. aut Blanco, M. D. aut Teijón, J. M. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 19(2000), 3 vom: 01. Apr., Seite 199-208 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:19 year:2000 number:3 day:01 month:04 pages:199-208 https://dx.doi.org/10.1023/A:1007055719926 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_120 GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 19 2000 3 01 04 199-208 |
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10.1023/A:1007055719926 doi (DE-627)SPR052715140 (SPR)A:1007055719926-e DE-627 ger DE-627 rakwb eng Socorro, J. M. verfasserin aut Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 2000 Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. Olmo, R. aut Teijón, C. aut Blanco, M. D. aut Teijón, J. M. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 19(2000), 3 vom: 01. Apr., Seite 199-208 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:19 year:2000 number:3 day:01 month:04 pages:199-208 https://dx.doi.org/10.1023/A:1007055719926 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_120 GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 19 2000 3 01 04 199-208 |
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Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. © Plenum Publishing Corporation 2000 |
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Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. © Plenum Publishing Corporation 2000 |
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Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. © Plenum Publishing Corporation 2000 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR052715140</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230812064831.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230812s2000 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1023/A:1007055719926</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR052715140</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)A:1007055719926-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Socorro, J. M.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2000</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Plenum Publishing Corporation 2000</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Olmo, R.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Teijón, C.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Blanco, M. D.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Teijón, J. M.</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">The protein journal</subfield><subfield code="d">Dordrecht : Springer Science + Business Media B.V., 2004</subfield><subfield code="g">19(2000), 3 vom: 01. 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