Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation.
about
Site-specific infrared probes of proteinsSelenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure.Comparison of biological chromophores: photophysical properties of cyanophenylalanine derivatives.Manipulation of enzyme properties by noncanonical amino acid incorporation.Molecular dynamics simulation of configurational ensembles compatible with experimental FRET efficiency data through a restraint on instantaneous FRET efficiencies.Spectroscopic studies of protein folding: linear and nonlinear methodsSensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligationp-Cyanophenylalanine and selenomethionine constitute a useful fluorophore-quencher pair for short distance measurements: application to polyproline peptides.Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules.Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.Quenching of p-Cyanophenylalanine Fluorescence by Various AnionsExploring protein lipidation with chemical biology.4-Cyano-α-methyl-l-phenylalanine as a spectroscopic marker for the investigation of peptaibiotic-membrane interactions.Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ(1-23) using an unnatural amino acid.Proline editing: a general and practical approach to the synthesis of functionally and structurally diverse peptides. Analysis of steric versus stereoelectronic effects of 4-substituted prolines on conformation within peptides.New aspects of the structure and mode of action of the human cathelicidin LL-37 revealed by the intrinsic probe p-cyanophenylalanine.pH-regulated selectivity in supramolecular polymerizations: switching between Co- and homopolymers.
P2860
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P2860
Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@ast
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@en
type
label
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@ast
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@en
prefLabel
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@ast
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@en
P2093
P2860
P356
P1433
P1476
Modulation of p-cyanophenylala ...... obes of alpha-helix formation.
@en
P2093
Daniel Goldberg
Humeyra Taskent-Sezgin
Isaac Carrico
Juah Chung
Peter Marek
Rosanne Thomas
P2860
P304
P356
10.1021/BI100932P
P407
P577
2010-07-01T00:00:00Z