| Autor: |
Andersen, K V, Ludvigsen, S, Mandrup, S, Knudsen, J, Poulsen, F M |
| Jazyk: |
angličtina |
| Rok vydání: |
1991 |
| Předmět: |
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| Zdroj: |
Andersen, K V, Ludvigsen, S, Mandrup, S, Knudsen, J & Poulsen, F M 1991, ' The secondary structure in solution of acyl-coenzyme A binding protein from bovine liver using 1H nuclear magnetic resonance spectroscopy ', Biochemistry, vol. 30, no. 44, pp. 10654-63 . https://doi.org/10.1021/bi00108a008 |
| DOI: |
10.1021/bi00108a008 |
| Popis: |
Acyl-coenzyme A binding protein from bovine liver and the protein expressed in Escherichia coli by the recombinant gene of this protein have been studied by two-dimensional 1H nuclear magnetic resonance spectroscopy. This protein has, in addition to the ability to bind acyl-coenzyme A, been reported to have several important physiological and biochemical functions. It is known as the diazepam binding inhibitor, as a putative neurotransmitter, as a regulator of insulin release from pancreatic cells, and as a mediator in corticotropin-dependent adrenal steroidogenesis. The only difference between the protein produced by recombinant techniques and the native acyl-coenzyme A binding protein is the N-terminal acetyl group present only in the native protein. The two proteins have 86 amino acid residues and a molecular mass of approximately 10,000 Da. Complete assignment of the 1H nuclear magnetic resonances has been obtained for a major proportion of the amino acid residues (55 residues), and partial assignment has been achieved for the others (31 residues). Sequential nuclear Overhauser effects have demonstrated that the protein has a secondary structure consisting of four alpha-helices of residues 1-15, 22-35, 52-60, and 68-85. Furthermore, a large number of long-range nuclear Overhauser effects have been identified, indicating that the assignment given here will provide a basis for a structure determination of this protein in solution by nuclear magnetic resonance spectroscopy. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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