Journal article
Conservation of amino acids in multiple alignments: aspartic acid has unexpected conservation
- Abstract:
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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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(Version of record, pdf, 616.9KB)
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- Publisher copy:
- 10.1016/S0014-5793(96)01181-7
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Funding
+ Paul and Daisy Soros Fellowships for New Americans
More from this funder
Funding agency for:
Fiser, A
Bibliographic Details
- 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:
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9601-2562
- ISSN:
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0014-5793
Item Description
- Language:
- English
- Keywords:
- Subjects:
- UUID:
-
uuid:d244ae73-0af5-494c-bd84-17cb3ed40d24
- Local pid:
- ora:8509
- Deposit date:
- 2014-06-03
Related Items
Terms of use
- Copyright holder:
- Federation of European Biochemical Societies
- Copyright date:
- 1996
- Notes:
- Copyright 1996 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Re-use of this article is permitted in accordance with the Terms and Conditions set out at http://www.elsevier.com/open-access/userlicense/1.0/
- Licence:
- Other
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