# Structural principles of α/β barrel proteins: The packing of the interior of the sheet

@article{Lesk1989StructuralPO,
title={Structural principles of $\alpha$/$\beta$ barrel proteins: The packing of the interior of the sheet},
author={Arthur M. Lesk and C. I. Br{\"a}nd{\'e}n and Cyrus Chothia},
journal={Proteins: Structure},
year={1989},
volume={5}
}
• Published 1989
• Chemistry
• Proteins: Structure
α/β barrel structures very similar to that first observed in triose phosphate isomerase are now known to occur in 14 enzymes. To understand the origin of this fold, we analyzed in three of these proteins the geometry of the eight‐stranded β‐sheets and the packing of the residues at the center of the barrel. The Packingin thisregion is seen in its simplest form in glycolate oxidase. It consists of 12 residues arranged in three layers. Each layer contains four side chains. The packing of RubisCO… Expand
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• Materials Science, Medicine
• Journal of molecular biology
• 1994
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Principles determining the structure of beta-sheet barrels in proteins. II. The observed structures.
• Physics, Medicine
• Journal of molecular biology
• 1994
The observed arrangement of the strands, and the extent of the twist and coiling of the beta-sheets, are very close to those calculated from the (n, S) values for the barrel, demonstrating the validity of these principles. Expand
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• Biology, Medicine
• Protein science : a publication of the Protein Society
• 1994
It is demonstrated that simple genetic alterations may be responsible for switching the nature of side‐chain packing observed in β/α‐barrels and that convergent evolution to a stable fold need not be invoked to account for the emergence of 2 classes of β/β-barrel core. Expand
Recurrent αβ loop structures in TIM barrel motifs show a distinct pattern of conserved structural features
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• Chemistry, Medicine
• Protein science : a publication of the Protein Society
• 1999
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• Biology
• 2004
This work proposes a new consensus approach for locating stabilizing residues in TIM‐barrel domains based on long‐range interactions, hydrophobicity, and conservation of amino acid residues, and suggests that these residues are among the ones with less mobility in the considered proteins. Expand
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• Chemistry, Medicine
• Protein science : a publication of the Protein Society
• 1999
The β‐sheet unit (βu), defined as a pair of adjacent parallel or antiparallel hydrogen‐bonded β‐strands, packing with an α‐helix shows a better correlation between the interaxial distance and log (V/nda) for the residues in the packing interface. Expand
The structure and evolution of a/β barrel proteins
• Chemistry, Medicine
• FASEB journal : official publication of the Federation of American Societies for Experimental Biology
• 1995
Arguments are made to support the divergence of all members of this family from a common ancestor and evidence is presented to suggest that convergent molecular evolution occurs when there is only one energetically reasonable pathway for a chemical reaction. Expand
One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
• Biology, Medicine
• Journal of molecular biology
• 2002
The eightfold barrel structure, first observed in triose-phosphate isomerase, occurs ubiquitously in nature and is an extreme example of the "one fold-many functions" paradigm, which illustrates the difficulty of assigning function through a structural genomics approach for some folds. Expand
Packing constraints of hydrophobic side chains in (α/β)8 barrels
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• 1995
An analysis of possible tight packing of hydrophobic groups simultaneously at the both surfaces of β‐hyperboloid‐8 was conducted. This analysis shows that the disposition of amino acid side chains atExpand

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