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  Polyphenylalanine synthesis by crystallized trypsin-modified EF-Tu · GDP

Wittinghofer, A., Frank, R., Gast, W. H., & Leberman, R. (1979). Polyphenylalanine synthesis by crystallized trypsin-modified EF-Tu · GDP. Journal of Molecular Biology (London), 132(2), 253-256. doi:10.1016/0022-2836(79)90394-2.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0004-50DA-C Version Permalink: https://hdl.handle.net/21.11116/0000-0004-50DB-B
Genre: Journal Article

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JMolBiol_132_1979_253.pdf (Any fulltext), 458KB
 
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 Creators:
Wittinghofer, Alfred1, Author           
Frank, Rainer2, Author           
Gast, Wolfgang H.2, Author           
Leberman, Reuben2, Author           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: The protein from orthorhombic and tetragonal crystals of trypsinized elongation factor Tu is as active as the native protein in stimulating polyphenylalanine synthesis and contains predominately the high and low molecular weight polypeptides, fragment A and fragment D. The protein from pseudotetragonal crystals, which is more degraded, is much less active in polyphenylalanine synthesis.

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Language(s): eng - English
 Dates: 1979-03-142001-11-021979-08-05
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0022-2836(79)90394-2
 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: 132 (2) Sequence Number: - Start / End Page: 253 - 256 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042