Probing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteines
about
Site-specific infrared probes of proteinsStructural disorder within paramyxoviral nucleoproteinsProbing the phosphopantetheine arm conformations of acyl carrier proteins using vibrational spectroscopy.One-step generation of error-prone PCR libraries using Gateway® technology.Expanding the proteome: disordered and alternatively folded proteins.Characterization of the interactions between the nucleoprotein and the phosphoprotein of HenipavirusDividing to unveil protein microheterogeneities: traveling wave ion mobility studySite-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules.Using infrared spectroscopy of cyanylated cysteine to map the membrane binding structure and orientation of the hybrid antimicrobial peptide CM15.Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy.Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy.Vibrational dynamics and solvatochromism of the label SCN in various solvents and hemoglobin by time dependent IR and 2D-IR spectroscopy.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.Conserved electrostatic fields at the Ras-effector interface measured through vibrational Stark effect spectroscopy explain the difference in tilt angle in the Ras binding domains of Raf and RalGDS.Cyanylated Cysteine Reports Site-Specific Changes at Protein-Protein-Binding Interfaces Without Perturbation.Synthesis of 5-Cyano-Tryptophan as a Two-Dimensional Infrared Spectroscopic Reporter of Structure.
P2860
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P2860
Probing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteines
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին 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
Probing structural transitions ...... oscopy of cyanylated cysteines
@ast
Probing structural transitions ...... oscopy of cyanylated cysteines
@en
Probing structural transitions ...... oscopy of cyanylated cysteines
@nl
type
label
Probing structural transitions ...... oscopy of cyanylated cysteines
@ast
Probing structural transitions ...... oscopy of cyanylated cysteines
@en
Probing structural transitions ...... oscopy of cyanylated cysteines
@nl
prefLabel
Probing structural transitions ...... oscopy of cyanylated cysteines
@ast
Probing structural transitions ...... oscopy of cyanylated cysteines
@en
Probing structural transitions ...... oscopy of cyanylated cysteines
@nl
P2093
P2860
P1433
P1476
Probing structural transitions ...... oscopy of cyanylated cysteines
@en
P2093
David M Snead
Elodie Terrer
Sonia Longhi
Stéphanie Costanzo
P2860
P304
P356
10.1016/J.BPJ.2010.06.060
P407
P577
2010-09-01T00:00:00Z