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Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)Solution Structure of an ABC Collagen Heterotrimer Reveals a Single-register Helix Stabilized by Electrostatic InteractionsInterfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains.Interfacial water molecules in SH3 interactions: a revised paradigm for polyproline recognition.The stiffness of collagen fibrils influences vascular smooth muscle cell phenotype.Synthesis of heterotrimeric collagen peptides containing the alpha1beta1 integrin recognition site of collagen type IV.NMR dispersion investigations of enzymatically degraded bovine articular cartilage.Hydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.The polyproline II conformation in short alanine peptides is noncooperativeThe effect of deuterium oxide on the stability of the collagen model peptides H-(Pro-Pro-Gly)(10)-OH, H-(Gly-Pro-4(R)Hyp)(9)-OH, and Type I collagen.Surface Engineering for Mechanical Enhancement of Cell Sheet by Nano-Coatings.Solid-state and unilateral NMR study of deterioration of a Dead Sea Scroll fragment.Structure and hydration of the DNA-human topoisomerase I covalent complex.Birefringence and second harmonic generation on tendon collagen following red linearly polarized laser irradiation.Spatio-temporal modification of collagen scaffolds mediated by triple helical propensity.Synthetic heterotrimeric collagen peptides as mimics of cell adhesion sites of the basement membrane.In vivo studies of ultrafast near-infrared laser tissue bonding and wound healing.Synthesis and biological applications of collagen-model triple-helical peptides.Investigating the relationship between changes in collagen fiber orientation during skin aging and collagen/water interactions by polarized-FTIR microimaging.Role of hydration in collagen recognition by bacterial adhesinsInteraction of the α2A domain of integrin with small collagen fragments.Single molecule effects of osteogenesis imperfecta mutations in tropocollagen protein domains.A (4R)- or a (4S)-fluoroproline residue in position Xaa of the (Xaa-Yaa-Gly) collagen repeat severely affects triple-helix formation.Material properties of historic parchment: A reference collection survey
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Hydration dynamics of the collagen triple helix by NMR.
@ast
Hydration dynamics of the collagen triple helix by NMR.
@en
type
label
Hydration dynamics of the collagen triple helix by NMR.
@ast
Hydration dynamics of the collagen triple helix by NMR.
@en
prefLabel
Hydration dynamics of the collagen triple helix by NMR.
@ast
Hydration dynamics of the collagen triple helix by NMR.
@en
P2093
P356
P1476
Hydration dynamics of the collagen triple helix by NMR
@en
P2093
P304
P356
10.1006/JMBI.2000.3919
P407
P577
2000-07-01T00:00:00Z