Vibrational Stark effect spectroscopy at the interface of Ras and Rap1A bound to the Ras binding domain of RalGDS reveals an electrostatic mechanism for protein-protein interaction.
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Biomolecular electrostatics and solvation: a computational perspectiveSite-specific infrared probes of proteinsQuantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase.Probing the phosphopantetheine arm conformations of acyl carrier proteins using vibrational spectroscopy.Site-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.Alkyl-Nitrile Adlayers as Probes of Plasmonically Induced Electric Fields.Imaging Electric Fields in SERS and TERS Using the Vibrational Stark Effect.Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.3-picolyl azide adenine dinucleotide as a probe of femtosecond to picosecond enzyme dynamics.Selective incorporation of nitrile-based infrared probes into proteins via cysteine alkylationMeasurement of the membrane dipole electric field in DMPC vesicles using vibrational shifts of p-cyanophenylalanine and molecular dynamics simulations.On the possible role of protein vibrations in information processing in the brain: three Russian dolls.Vibrational solvatochromism: towards systematic approach to modeling solvation phenomena.Conformational Ensembles of Calmodulin Revealed by Nonperturbing Site-Specific Vibrational Probe Groups.Intrinsic electric fields in ionic liquids determined by vibrational Stark effect spectroscopy and molecular dynamics simulation.Vibrational dynamics and solvatochromism of the label SCN in various solvents and hemoglobin by time dependent IR and 2D-IR spectroscopy.Vibrational Stark effect spectroscopy reveals complementary electrostatic fields created by protein-protein binding at the interface of Ras and Ral.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.Vibrational solvatochromism of nitrile infrared probes: beyond the vibrational Stark dipole approach.Cyanylated Cysteine Reports Site-Specific Changes at Protein-Protein-Binding Interfaces Without Perturbation.
P2860
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P2860
Vibrational Stark effect spectroscopy at the interface of Ras and Rap1A bound to the Ras binding domain of RalGDS reveals an electrostatic mechanism for protein-protein interaction.
description
2010 nî lūn-bûn
@nan
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
2010年论文
@zh
2010年论文
@zh-cn
name
Vibrational Stark effect spect ...... r protein-protein interaction.
@en
Vibrational Stark effect spect ...... r protein-protein interaction.
@nl
type
label
Vibrational Stark effect spect ...... r protein-protein interaction.
@en
Vibrational Stark effect spect ...... r protein-protein interaction.
@nl
prefLabel
Vibrational Stark effect spect ...... r protein-protein interaction.
@en
Vibrational Stark effect spect ...... r protein-protein interaction.
@nl
P2093
P356
P1476
Vibrational Stark effect spect ...... r protein-protein interaction.
@en
P2093
Amy J Stafford
Daniel L Ensign
Lauren J Webb
P304
15331-15344
P356
10.1021/JP106974E
P407
P577
2010-10-22T00:00:00Z