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  Complete 1H nuclear magnetic resonance assignments and structural characterization of a fusion protein of the alpha-amylase inhibitor tendamistat with the activation domain of the human immunodeficiency virus type 1 Tat protein

Freund, J., Vértesy, L., Koller, K.-P., Wolber, V., Heintz, D., & Kalbitzer, H. R. (1995). Complete 1H nuclear magnetic resonance assignments and structural characterization of a fusion protein of the alpha-amylase inhibitor tendamistat with the activation domain of the human immunodeficiency virus type 1 Tat protein. Journal of Molecular Biology (London), 250(5), 672-688. doi:10.1006/jmbi.1995.0407.

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Genre: Journal Article
Alternative Title : Complete 1H nuclear magnetic resonance assignments and structural characterization of a fusion protein of the α-amylase inhibitor tendamistat with the activation domain of the human

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JMolBiol_250_1995_672.pdf (Any fulltext), 2MB
 
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 Creators:
Freund, Jens1, Author              
Vértesy, László, Author
Koller, Klaus-Peter, Author
Wolber, Vera1, Author              
Heintz, Daniela1, Author              
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: HIV-1 Tat; tendamistat; hydrogen bonds; fusion protein; NMR structure
 Abstract: Complete sequence-specific assignments of the 1H-NMR spectrum of a fusion protein of the alpha-amylase inhibitor tendamistat from Streptomyces tendae and the activation domain of Tat from human immunodeficiency virus type 1 (HIV-1) was obtained by homonuclear two-dimensional NMR methods. The protein behaves as expected for an ideal fusion protein: the flexible linker allows an almost completely decoupled motion of the subunits of the protein and the two subunits show almost no mutual interaction. In the tendamistat part, small structural distortions due to exchange of the carboxy-terminal leucine propagate mainly via the hydrogen bonds of the beta-sheet and the disulfide bond. The Tat part of the protein contains the seven cysteine residues of full-length Tat. The fusion protein was expressed in Streptomyces lividans and exported. During the export to the extracellular space disulfide bonds are created by the expressing cells, only one sulfhydryl group remains accessible for sulfhydryl reagents. Although a unique, dominant conformation with a specific disulfide bonding pattern exists, a significant conformational variation can be observed including cis-proline peptide bonds, which may indicate smaller populations with alternative disulfide bonding patterns.

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Language(s): eng - English
 Dates: 1995-01-181995-05-121995-07-28
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 250 (5) Sequence Number: - Start / End Page: 672 - 688 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042