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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Proteins Structure F...arrow_drop_down
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Proteins Structure Function and Bioinformatics
Article . 1995 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
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Prediction of the structure of GroES and its interaction with GroEL

Authors: Valencia, A; Hubbard, T J; Muga, A; Bañuelos, S; Llorca, O; Carrascosa, J L; Valpuesta, J M;

Prediction of the structure of GroES and its interaction with GroEL

Abstract

AbstractThe three‐dimensional structure of the GroES monomer and its interaction with GroEL has been predicted using a combination of prediction tools and experimental data obtained by biophysical [electron microscope (EM), Fourier transform infrared (FTIR), and nuclear magnetic resonance (NMR)] and biochemical techniques. The GroES monomer, according to the prediction, is composed of eight β‐strands forming a β‐barrel with loose ends. In the model, β‐strands 5–8 run along the outer surface of GroES, forming an antiparallel β‐sheet with β4 loosely bound to one of the edges. β‐strands 1–3 would then be parallel and placed in the interior of the molecule. Loops 1–3 would face the internal cavity of the GroEL–GroES complex, and together with conserved residues in loops 5 and 7, would form the active surface interacting with GroEL. © 1995 Wiley‐Liss, Inc.

Country
United Kingdom
Keywords

Models, Molecular, Protein Structure, Secondary, Protein Folding, Magnetic Resonance Spectroscopy, Databases, Factual, Protein Conformation, Molecular Sequence Data, Electron, Protein Structure, Secondary, Databases, Models, Spectroscopy, Fourier Transform Infrared, Chaperonin 10, Amino Acid Sequence, Factual, Spectroscopy, Conserved Sequence, Microscopy, Binding Sites, Molecular, Chaperonin 60, 540, Recombinant Proteins, Microscopy, Electron, Fourier Transform Infrared, Mutation

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
14
Average
Average
Top 10%
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