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  Predicted secondary structure of the 20 S proteasome and model structure of the putative peptide channel

Lupas, A., Koster, A. J., Walz, J., & Baumeister, W. (1994). Predicted secondary structure of the 20 S proteasome and model structure of the putative peptide channel. FEBS Letters., 354(1), 45-49.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-739D-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-739E-1
Genre: Journal Article

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 Creators:
Lupas, A.1, Author              
Koster, A. J.1, Author              
Walz, J.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Amino Acid Sequence; Computer Simulation; *Cysteine Endopeptidases/ch [Chemistry]; Cysteine Endopeptidases/ge [Genetics]; Cysteine Endopeptidases/ul [Ultrastructure]; *Models, Molecular; Molecular Sequence Data; *Multienzyme Complexes/ch [Chemistry]; Multienzyme Complexes/ge [Genetics]; Multienzyme Complexes/ul [Ultrastructure]; *Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; *Thermoplasma/ch [Chemistry]
 Abstract: Secondary structure prediction has made great progress in recent years due to the incorporation of evolutionary information, and may be close to a point where (in combination with biochemical and low-resolution structural data) it can guide the modelling of tertiary structure in cases where no model building is possible by homology. Towards this goal it is important to gather information on the performance of prediction methods in advance of the publication of new structures. In anticipation of the soon-to-be-released structure of the 20 S proteasome from Thermoplasma acidophilum, we have applied several widely used secondary structure prediction methods to proteasome sequences and have attempted to model the putative channel in the outer proteasome rings (alpha-rings) based on the obtained predictions.

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 Dates: 1994
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 318675
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Title: FEBS Letters.
Source Genre: Journal
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Pages: - Volume / Issue: 354 (1) Sequence Number: - Start / End Page: 45 - 49 Identifier: -