Sparsely populated residue conformations in protein structures: revisiting "experimental" Ramachandran maps.

Sparsely populated residue conformations in protein structures: revisiting "experimental" Ramachandran maps.

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http://www.wikidata.org/entity/Q38128264
Native proteins trap high-energy transit conformations3d interaction homology: The structurally known rotamers of tyrosine derive from a surprisingly limited set of information-rich hydropathic interaction environments described by maps.The determinants of bond angle variability in protein/peptide backbones: A comprehensive statistical/quantum mechanics analysis.Extension of the classical classification of β-turns.En route towards the peptide γ-helix: X-ray diffraction analyses and conformational energy calculations of Adm-rich short peptides.Insights into resistance mechanism of the macrolide biosensor protein MphR(A) binding to macrolide antibiotic erythromycin by molecular dynamics simulation.Dihedral angle preferences of amino acid residues forming various non-local interactions in proteins.Single and multiple peptide γ-turns: literature survey and recent progress
P2860

Sparsely populated residue conformations in protein structures: revisiting "experimental" Ramachandran maps.

Item
http://www.wikidata.org/entity/Q38128264
description
article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Sparsely populated residue con ...... perimental" Ramachandran maps.
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type
label
Sparsely populated residue con ...... perimental" Ramachandran maps.
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prefLabel
Sparsely populated residue con ...... perimental" Ramachandran maps.
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P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Sparsely populated residue con ...... perimental" Ramachandran maps.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698