Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics.
about
Site-specific infrared probes of proteinsProbing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study.Azido Homoalanine is a Useful Infrared Probe for Monitoring Local Electrostatistics and Sidechain Solvation in Proteins.Bioorthogonal chemical reporters for analyzing protein lipidation and lipid traffickingPulse-chase analysis of procollagen biosynthesis by azidohomoalanine labeling.Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules.New method for the orthogonal labeling and purification of Toxoplasma gondii proteins while inside the host cellTwo-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligandThe Role of Electrostatic Interactions in Folding of β-ProteinsTwo-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes.Two-Dimensional Infrared Study of Vibrational Coupling between Azide and Nitrile Reporters in a RNA NucleosideA direct comparison of azide and nitrile vibrational probesSynthesis and Protein Incorporation of Azido-Modified Unnatural Amino Acids.Modulating Accidental Fermi Resonance: What a Difference a Neutron MakesSensitive, site-specific, and stable vibrational probe of local protein environments: 4-azidomethyl-L-phenylalanine.A solvatochromic model calibrates nitriles' vibrational frequencies to electrostatic fields.General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins.Site-selective azide incorporation into endogenous RNase A via a "chemistry" approach.Vibrational solvatochromism: towards systematic approach to modeling solvation phenomena.Impact of Azidohomoalanine Incorporation on Protein Structure and Ligand Binding.The covalently bound diazo group as an infrared probe for hydrogen bonding environments.Solvation dynamics of an ionic probe in choline chloride-based deep eutectic solvents.Vibrational dynamics and solvatochromism of the label SCN in various solvents and hemoglobin by time dependent IR and 2D-IR spectroscopy.Optimizing immobilization of avidin on surface-modified magnetic nanoparticles: characterization and application of protein-immobilized nanoparticles.Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine.Synthesis of 5-Cyano-Tryptophan as a Two-Dimensional Infrared Spectroscopic Reporter of Structure.
P2860
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P2860
Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին 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
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@ast
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@en
type
label
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@ast
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@en
prefLabel
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@ast
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@en
P2093
P2860
P356
P1476
Azidohomoalanine: a conformati ...... structure, and electrostatics.
@en
P2093
Humeyra Taskent-Sezgin
Isaac Carrico
Juah Chung
Partha S Banerjee
R Brian Dyer
Sureshbabu Nagarajan
P2860
P304
P356
10.1002/ANIE.201003325
P407
P577
2010-10-01T00:00:00Z