Les interactions proteine-proteine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique
The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The proble...
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E-Artikel |
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| Sprache: |
Französisch |
| Erschienen: |
1986 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimie - Amsterdam : Elsevier, 68(1986), 3, Seite 395-400 |
| Übergeordnetes Werk: |
volume:68 ; year:1986 ; number:3 ; pages:395-400 |
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| 520 | |a The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? | ||
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(DE-627)NLEJ177262826 (DE-599)GBVNLZ177262826 DE-627 ger DE-627 rakwb fre Les interactions proteine-proteine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Maire, M.l. oth in Biochimie Amsterdam : Elsevier 68(1986), 3, Seite 395-400 (DE-627)NLEJ177262761 (DE-600)2011725-5 0300-9084 nnns volume:68 year:1986 number:3 pages:395-400 http://dx.doi.org/10.1016/S0300-9084(86)80006-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1986 3 395-400 |
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(DE-627)NLEJ177262826 (DE-599)GBVNLZ177262826 DE-627 ger DE-627 rakwb fre Les interactions proteine-proteine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Maire, M.l. oth in Biochimie Amsterdam : Elsevier 68(1986), 3, Seite 395-400 (DE-627)NLEJ177262761 (DE-600)2011725-5 0300-9084 nnns volume:68 year:1986 number:3 pages:395-400 http://dx.doi.org/10.1016/S0300-9084(86)80006-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1986 3 395-400 |
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(DE-627)NLEJ177262826 (DE-599)GBVNLZ177262826 DE-627 ger DE-627 rakwb fre Les interactions proteine-proteine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Maire, M.l. oth in Biochimie Amsterdam : Elsevier 68(1986), 3, Seite 395-400 (DE-627)NLEJ177262761 (DE-600)2011725-5 0300-9084 nnns volume:68 year:1986 number:3 pages:395-400 http://dx.doi.org/10.1016/S0300-9084(86)80006-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1986 3 395-400 |
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(DE-627)NLEJ177262826 (DE-599)GBVNLZ177262826 DE-627 ger DE-627 rakwb fre Les interactions proteine-proteine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Maire, M.l. oth in Biochimie Amsterdam : Elsevier 68(1986), 3, Seite 395-400 (DE-627)NLEJ177262761 (DE-600)2011725-5 0300-9084 nnns volume:68 year:1986 number:3 pages:395-400 http://dx.doi.org/10.1016/S0300-9084(86)80006-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1986 3 395-400 |
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(DE-627)NLEJ177262826 (DE-599)GBVNLZ177262826 DE-627 ger DE-627 rakwb fre Les interactions proteine-proteine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Maire, M.l. oth in Biochimie Amsterdam : Elsevier 68(1986), 3, Seite 395-400 (DE-627)NLEJ177262761 (DE-600)2011725-5 0300-9084 nnns volume:68 year:1986 number:3 pages:395-400 http://dx.doi.org/10.1016/S0300-9084(86)80006-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 68 1986 3 395-400 |
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The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? |
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The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? |
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The organization of polypeptide chains in the membrane has attracted widespread interest. This is particularly true for transport proteins: indeed, the existence of a quaternary structure may obviously have important implications for the mechanism of solute transport through the membrane. The problem arises from the fact that it is extremely difficult to demonstrate unambiguously that a protein is truly oligomeric in the membrane. In this paper various techniques are considered, either direct methods of investigation such as X-ray or neutron scattering, ESR, and radiation inactivation, or indirect methods (primarily the solubilization of the protein by non-denaturing detergents). In very few cases the existence of a 'structural' oligomer has been demonstrated. However, the question remains whether the oligomer also has a functional role, i.e., is it directly necessary for example to form a hydrophilic pathway for an ion, or indirectly to stabilize the enzyme structure or to allow a control to take place at a certain defined step of the transport cycle? |
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