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Conservation of amino acids in multiple alignments: aspartic acid has unexpected conservation

Abstract:

Analysis of the relationship between surface accessibility and amino acid conservation in multiple sequence alignments of homologous proteins confirms expected trends for hydrophobic amino acids, but reveals an unexpected difference between the conservation of Asp, Glu and Gln. Even when not in an active site, Asp is more highly conserved than Glu. There is a clear preference for conserved and buried Asp to be present in coil, but there is no tendency for Asp to conserve φ/ψ in the ++ regi...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/S0014-5793(96)01181-7

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Institution:
Hungarian Academy of Sciences
Department:
Institute of Enzymology
Role:
Author
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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author

Contributors

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Funding agency for:
Barton, G
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Funding agency for:
Barton, G
Publisher:
Elsevier Publisher's website
Journal:
FEBS Letters Journal website
Volume:
397
Issue:
2-3
Pages:
225-229
Publication date:
1996-11-01
DOI:
EISSN:
9601-2562
ISSN:
0014-5793
Language:
English
Keywords:
Subjects:
UUID:
uuid:d244ae73-0af5-494c-bd84-17cb3ed40d24
Local pid:
ora:8509
Deposit date:
2014-06-03

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