دورية أكاديمية
أعرض في EDS

Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.

التفاصيل البيبلوغرافية
العنوان: Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.
المؤلفون: Thielges MC; Department of Chemistry, Stanford University, Stanford, California 94305, USA., Axup JY, Wong D, Lee HS, Chung JK, Schultz PG, Fayer MD
المصدر: The journal of physical chemistry. B [J Phys Chem B] 2011 Sep 29; Vol. 115 (38), pp. 11294-304. Date of Electronic Publication: 2011 Aug 31.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101157530 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5207 (Electronic) Linking ISSN: 15205207 NLM ISO Abbreviation: J Phys Chem B Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c1997-
مواضيع طبية MeSH: Molecular Dynamics Simulation*, Amino Acids/*chemistry , Myoglobin/*chemistry , Spectrophotometry, Infrared/*methods, Amino Acid Substitution ; Amino Acids/genetics ; Azides/chemistry ; Carbon Monoxide/chemistry ; Heme/chemistry ; Ligands ; Mutation ; Myoglobin/genetics ; Protein Binding ; Protein Conformation ; Spectroscopy, Fourier Transform Infrared ; Vibration
مستخلص: 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.
(© 2011 American Chemical Society)
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معلومات مُعتمدة: R01 GM062159 United States GM NIGMS NIH HHS; R0162159 United States PHS HHS; 2-R01-GM061137-09 United States GM NIGMS NIH HHS; R01 GM062159-11 United States GM NIGMS NIH HHS; F32-GM090549 United States GM NIGMS NIH HHS; R01 GM061137-12 United States GM NIGMS NIH HHS; F32 GM090549 United States GM NIGMS NIH HHS; R01 GM061137 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Amino Acids)
0 (Azides)
0 (Ligands)
0 (Myoglobin)
42VZT0U6YR (Heme)
7U1EE4V452 (Carbon Monoxide)
تواريخ الأحداث: Date Created: 20110810 Date Completed: 20120207 Latest Revision: 20240610
رمز التحديث: 20240610
مُعرف محوري في PubMed: PMC3261801
DOI: 10.1021/jp206986v
PMID: 21823631
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5207
DOI:10.1021/jp206986v