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Science 17 June 1988: Vol. 240. no. 4859, pp. 1648 - 1652 DOI: 10.1126/science.3381086
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Articles
Science, Vol 240, Issue 4859, 1648-1652
Copyright © 1988 by American Association for the Advancement of Science
Amino acid preferences for specific locations at the ends of alpha helices
JS Richardson
and
DC Richardson
Department of Biochemistry, Duke University, Durham, NC 27710.
A definition based on alpha-carbon positions and a sample of 215 alpha helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.
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- Crystallographic citations.
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Science
242, 347
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Science
240, 1632-1641
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J. Biol. Chem.
275, 24630-24638
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- Requirement of Specific Intrahelical Interactions for Stabilizing the Inactive Conformation of Glycoprotein Hormone Receptors.
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J. Biol. Chem.
275, 37860-37869
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- O-helix Mutant T664P of Thermus aquaticus DNA Polymerase I. ALTERED CATALYTIC PROPERTIES FOR INCORPORATION OF INCORRECT NUCLEOTIDES BUT NOT CORRECT NUCLEOTIDES.
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276, 27562-27567
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- The Folding and Stability of Human Alpha Class Glutathione Transferase A1-1 Depend on Distinct Roles of a Conserved N-capping Box and Hydrophobic Staple Motif.
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276, 32177-32183
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- The Crystal Structure of Indoleglycerol-phosphate Synthase from Thermotoga maritima. KINETIC STABILIZATION BY SALT BRIDGES.
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277, 8626-8634
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- Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha -helices.
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PNAS
98, 10670-10675
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