ArticleThe journal of physical chemistry. B2011
Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- Extracting accurate infrared lineshapes from weak vibrational probes at low concentrations.MethodsX · 2023Article
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- Increasing Pump-Probe Signal toward Asymptotic Limits.The journal of physical chemistry. B · 2023Review
- Versatile Vibrational Energy Sensors for Proteins.Angewandte Chemie (International ed. in English) · 2022Article
- Least-Squares Fitting of Multidimensional Spectra to Kubo Line-Shape Models.The journal of physical chemistry. B · 2021Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction.Chemical reviews · 2020Review
- Oscillatory Active-site Motions Correlate with Kinetic Isotope Effects in Formate Dehydrogenase.ACS catalysis · 2019Article
- Non-Additive Effects of Binding Site Mutations in Calmodulin.Biochemistry · 2019Article
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- Isonitrile-Derivatized Indole as an Infrared Probe for Hydrogen-Bonding Environments.Molecules (Basel, Switzerland) · 2019Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
- Site-specific 2D IR spectroscopy: a general approach for the characterization of protein dynamics with high spatial and temporal resolution.Physical chemistry chemical physics : PCCP · 2019Article
- Do Osmolytes Impact the Structure and Dynamics of Myoglobin?Molecules (Basel, Switzerland) · 2018Article
- Conformation-specific detection of calmodulin binding using the unnatural amino acid p-azido-phenylalanine (AzF) as an IR-sensor.Structural dynamics (Melville, N.Y.) · 2018Article
- Crystal structures of green fluorescent protein with the unnatural amino acid 4-nitro-L-phenylalanine.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Cyanylated Cysteine Reports Site-Specific Changes at Protein-Protein-Binding Interfaces Without Perturbation.Biochemistry · 2018Article
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Abstract
Protein dynamics and interactions in myoglobin (Mb) were characterized via two vibrational dynamics labels (VDLs): a genetically incorporated site-specific azide (Az) bearing unnatural amino acid (AzPhe43) and an active site CO ligand. The Az-labeled protein was studied using ultrafast two-dimensional infrared (2D IR) vibrational echo spectroscopy. CO bound at the active site of the heme serves as a second VDL located nearby. Therefore, it was possible to use Fourier transform infrared (FT-IR) and 2D IR spectroscopic experiments on the Az in unligated Mb and in Mb bound to CO (MbAzCO) and on the CO in MbCO and MbAzCO to investigate the environment and motions of different states of one protein from the perspective of two spectrally resolved VDLs. A very broad bandwidth 2D IR spectrum, encompassing both the Az and CO spectral regions, found no evidence of direct coupling between the two VDLs. In MbAzCO, both VDLs reported similar time scale motions: very fast homogeneous dynamics, fast, ∼1 ps dynamics, and dynamics on a much slower time scale. Therefore, each VDL reports independently on the protein dynamics and interactions, and the measured dynamics are reflective of the protein motions rather than intrinsic to the chemical nature of the VDL. The AzPhe VDL also permitted study of oxidized Mb dynamics, which could not be accessed previously with 2D IR spectroscopy. The experiments demonstrate that the combined application of 2D IR spectroscopy and site-specific incorporation of VDLs can provide information on dynamics, structure, and interactions at virtually any site throughout any protein.
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