Conformational stability of collagen relies on a stereoelectronic effect.
about
Collagen structure and stabilityProlyl 4-hydroxylaseChemoselectivity in chemical biology: acyl transfer reactions with sulfur and seleniumCrystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3)Stabilization of the collagen triple helix by O-methylation of hydroxyproline residuesReview collagen-based biomaterials for wound healingAsparagine beta-hydroxylation stabilizes the ankyrin repeat domain foldPreferred proline puckerings in cis and trans peptide groups: implications for collagen stabilityBacterial collagen-like proteins that form triple-helical structuresSynthesis and evaluation of a (3R,6S,9S)-2-oxo-1-azabicyclo[4.3.0]nonane scaffold as a mimic of Xaa-trans-Pro in poly-L-proline type II helix conformation.The impact of either 4-R-hydroxyproline or 4-R-fluoroproline on the conformation and SH3m-cort binding of HPK1 proline-rich peptide.Atomic polarizability dominates the electronic properties of peptide bonds upon thioxo or selenoxo substitution.An electronic effect on protein structure.Cotranslational incorporation of a structurally diverse series of proline analogues in an Escherichia coli expression system.Modulating the folding stability and ligand binding affinity of Pin1 WW domain by proline ring puckering.Energetics of an n --> pi interaction that impacts protein structure.The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contextsRational design of protein stability: effect of (2S,4R)-4-fluoroproline on the stability and folding pathway of ubiquitinHydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.2005 Emil Thomas Kaiser Award.4R- and 4S-iodophenyl hydroxyproline, 4R-pentynoyl hydroxyproline, and S-propargyl-4-thiolphenylalanine: conformationally biased and tunable amino acids for bioorthogonal reactions.O-acylation of hydroxyproline residues: effect on peptide-bond isomerization and collagen stability.New strategies for the design of folded peptoids revealed by a survey of noncovalent interactions in model systems4-chloroprolines: synthesis, conformational analysis, and effect on the collagen triple helixConformational preferences of substrates for human prolyl 4-hydroxylaseControl of Collagen Stability and Heterotrimer Specificity through Repulsive Electrostatic Interactions.De novo self-assembling collagen heterotrimers using explicit positive and negative design.The contribution of interchain salt bridges to triple-helical stability in collagen.The aberrance of the 4S diastereomer of 4-hydroxyproline.Self-assembly of synthetic collagen triple helices.Conformational changes associated with post-translational modifications of Pro(143) in Skp1 of Dictyostelium--a dipeptide model system.Spatio-temporal modification of collagen scaffolds mediated by triple helical propensity.Interstrand dipole-dipole interactions can stabilize the collagen triple helix.Quantum mechanical investigation of the effect of catalyst fluorination in the intermolecular asymmetric Stetter reaction.Metal ion-assembled micro-collagen heterotrimersEngineering D-Amino Acid Containing Collagen Like Peptide at the Cleavage Site of Clostridium histolyticum Collagenase for Its Inhibition.Thioamides in the collagen triple helixSynthesis of conformationally constrained 5-fluoro- and 5-hydroxymethanopyrrolidines. Ring-puckered mimics of gauche- and anti-3-fluoro- and 3-hydroxypyrrolidines.A Single Stereodynamic Center Modulates the Rate of Self-Assembly in a Biomolecular System.Is glycine a surrogate for a D-amino acid in the collagen triple helix?
P2860
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P2860
Conformational stability of collagen relies on a stereoelectronic effect.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Conformational stability of collagen relies on a stereoelectronic effect.
@en
Conformational stability of collagen relies on a stereoelectronic effect.
@nl
type
label
Conformational stability of collagen relies on a stereoelectronic effect.
@en
Conformational stability of collagen relies on a stereoelectronic effect.
@nl
prefLabel
Conformational stability of collagen relies on a stereoelectronic effect.
@en
Conformational stability of collagen relies on a stereoelectronic effect.
@nl
P2093
P356
P1476
Conformational stability of collagen relies on a stereoelectronic effect.
@en
P2093
Bretscher LE
DeRider ML
Jenkins CL
P304
P356
10.1021/JA005542V
P407
P577
2001-01-01T00:00:00Z