Effect of the N3 residue on the stability of the alpha-helix.
about
Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1Mapping side chain interactions at protein helix termini.The CXXC motif at the N terminus of an alpha-helical peptide.Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.Extrinsic interactions dominate helical propensity in coupled binding and folding of the lactose repressor protein hinge helix.Contributions of conserved TPLH tetrapeptides to the conformational stability of ankyrin repeat proteins.Local and macroscopic electrostatic interactions in single α-helices.The helical alanine controversy: an (Ala)6 insertion dramatically increases helicity.End-to-end and end-to-middle interhelical interactions: new classes of interacting helix pairs in protein structures.
P2860
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P2860
Effect of the N3 residue on the stability of the alpha-helix.
description
2004 nî lūn-bûn
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年论文
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2004年论文
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2004年论文
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name
Effect of the N3 residue on the stability of the alpha-helix.
@ast
Effect of the N3 residue on the stability of the alpha-helix.
@en
type
label
Effect of the N3 residue on the stability of the alpha-helix.
@ast
Effect of the N3 residue on the stability of the alpha-helix.
@en
prefLabel
Effect of the N3 residue on the stability of the alpha-helix.
@ast
Effect of the N3 residue on the stability of the alpha-helix.
@en
P2860
P356
P1433
P1476
Effect of the N3 residue on the stability of the alpha-helix
@en
P2093
Teuku M Iqbalsyah
P2860
P356
10.1110/PS.03341804
P577
2004-01-01T00:00:00Z