Temat: "NUCLEAR magnetic resonance" - OpacWWW

Skocz do pozycji: 1.

Tytuł:: Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils.
Autorzy:: Fonda BD; Department of Chemistry, University of California, Davis, California, USA.
Kato M; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Li Y; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Murray DT; Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA.; Pokaż więcej
Źródło:: Protein science : a publication of the Protein Society [Protein Sci] 2024 Oct; Vol. 33 (10), pp. e5168.
Typ publikacji:: Journal Article
MeSH Terms:: Cryoelectron Microscopy*/methods
Nuclear Magnetic Resonance, Biomolecular*/methods
Tropomyosin*/chemistry
Tropomyosin*/ultrastructure
Models, Molecular ; Protein Structure, Secondary ; Protein Conformation

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Tytuł:: Expanding the tool box for native structural biology: F dynamic nuclear polarization with fast magic angle spinning.
Autorzy:: Movellan KT; Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.
Zhu W; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.; Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.
Banks D; Bruker Biospin Corporation, 15 Fortune Drive, Billerica, MA 01821, USA.
Kempf J; Bruker Biospin Corporation, 15 Fortune Drive, Billerica, MA 01821, USA.
Runge B; Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.
Gronenborn AM; Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.; Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.; Department of Bioengineering, Swanson School of Engineering, University of Pittsburgh, Pittsburgh, PA 15261, USA.; Department of Chemistry, Dietrich School of Arts and Sciences, University of Pittsburgh, Pittsburgh, PA 15261, USA.
Polenova T; Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.; Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.; Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, PA 15261, USA.; Pokaż więcej
Źródło:: Science advances [Sci Adv] 2024 Oct 04; Vol. 10 (40), pp. eadq3115. Date of Electronic Publication: 2024 Oct 02.
Typ publikacji:: Journal Article
MeSH Terms:: SARS-CoV-2*/chemistry
Nuclear Magnetic Resonance, Biomolecular*/methods
Humans ; Fluorine/chemistry ; Viral Proteins/chemistry ; Viral Proteins/metabolism ; Magnetic Resonance Spectroscopy/methods ; COVID-19/virology

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Tytuł:: Lysine methylation: A strategy to improve in-cell NMR spectroscopy of proteins.
Autorzy:: Xiao X; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Zhan J; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Liu B; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan, 430074, China.
Zhu Q; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China.
Wang G; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China.
Zeng D; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Liu C; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Jiang B; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China; Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan, 430074, China.
He L; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Gong Z; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Zhou X; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China; Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan, 430074, China; Optics Valley Laboratory, Wuhan, 430074, China.
Zhang X; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China; Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan, 430074, China; Optics Valley Laboratory, Wuhan, 430074, China. Electronic address: .
Liu M; Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement of Science and Technology, Chinese Academy of Sciences, Wuhan, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China; Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan, 430074, China; Optics Valley Laboratory, Wuhan, 430074, China. Electronic address: .; Pokaż więcej
Źródło:: Analytica chimica acta [Anal Chim Acta] 2024 Oct 02; Vol. 1324, pp. 343099. Date of Electronic Publication: 2024 Aug 13.
Typ publikacji:: Journal Article
MeSH Terms:: Lysine*/chemistry
Lysine*/analysis
Nuclear Magnetic Resonance, Biomolecular*
Methylation ; Proteins/chemistry ; Proteins/analysis ; Humans

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Tytuł:: Protocol to perform fragment screening using NMR spectroscopy.
Autorzy:: Huang Q; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A∗STAR), Singapore 138670, Singapore.
Kang C; Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A∗STAR), Singapore 138670, Singapore. Electronic address: kang_.; Pokaż więcej
Źródło:: STAR protocols [STAR Protoc] 2024 Sep 20; Vol. 5 (3), pp. 103278. Date of Electronic Publication: 2024 Aug 22.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*/methods
Magnetic Resonance Spectroscopy/methods ; Ligands ; Binding Sites ; Proto-Oncogene Proteins p21(ras)/genetics ; Proto-Oncogene Proteins p21(ras)/chemistry ; Proto-Oncogene Proteins p21(ras)/metabolism ; Drug Discovery/methods ; Humans

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Tytuł:: Conformational dependence of chemical shifts in the proline rich region of TAU protein.
Autorzy:: Stöckelmaier J; Institute of Molecular Modeling and Simulation (MMS), University of Natural Resources and Life Sciences, Vienna, Austria. .
Oostenbrink C; Institute of Molecular Modeling and Simulation (MMS), University of Natural Resources and Life Sciences, Vienna, Austria. .; Pokaż więcej
Źródło:: Physical chemistry chemical physics : PCCP [Phys Chem Chem Phys] 2024 Sep 18; Vol. 26 (36), pp. 23856-23870. Date of Electronic Publication: 2024 Sep 18.
Typ publikacji:: Journal Article
MeSH Terms:: tau Proteins*/chemistry
Proline*/chemistry
Protein Conformation*
Nuclear Magnetic Resonance, Biomolecular*
Intrinsically Disordered Proteins/chemistry ; Humans

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Tytuł:: Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure.
Autorzy:: Rua AJ; Department of Molecular and Cellular Biology, University of Connecticut, Storrs, Connecticut, USA.
Alexandrescu AT; Department of Molecular and Cellular Biology, University of Connecticut, Storrs, Connecticut, USA.; Pokaż więcej
Źródło:: Protein science : a publication of the Protein Society [Protein Sci] 2024 Sep; Vol. 33 (9), pp. e5149.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*
Transcription Factors*/chemistry
Transcription Factors*/genetics
Transcription Factors*/metabolism
Zinc Fingers*
Humans ; Binding Sites ; Models, Molecular ; Protein Domains ; Zinc/metabolism ; Zinc/chemistry

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Tytuł:: Unveiling Charge-Pair Salt-Bridge Interaction Between GAGs and Collagen Protein in Cartilage: Atomic Evidence from DNP-Enhanced ssNMR at Natural Isotopic Abundance.
Autorzy:: Dwivedi N; Centre of Biomedical Research, SGPGIMS Campus, Raebareli Road, Lucknow 226014, India.
Patra B; Centre of Biomedical Research, SGPGIMS Campus, Raebareli Road, Lucknow 226014, India.; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.
Mentink-Vigier F; National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, United States.
Wi S; National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, United States.
Sinha N; Centre of Biomedical Research, SGPGIMS Campus, Raebareli Road, Lucknow 226014, India.; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.; Pokaż więcej
Źródło:: Journal of the American Chemical Society [J Am Chem Soc] 2024 Aug 28; Vol. 146 (34), pp. 23663-23668. Date of Electronic Publication: 2024 Jul 09.
Typ publikacji:: Journal Article
MeSH Terms:: Collagen*/chemistry
Collagen*/metabolism
Glycosaminoglycans*/chemistry
Glycosaminoglycans*/metabolism
Cartilage*/metabolism
Cartilage*/chemistry
Nuclear Magnetic Resonance, Biomolecular*
Animals ; Hydroxyproline/chemistry ; Hydrogen Bonding ; Salts/chemistry

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Skocz do pozycji: 8.

Tytuł:: Fluorinated Tags to Study Protein Conformation and Interactions Using F NMR.
Autorzy:: Hanson GSM; EaStChem School of Chemistry, University of Edinburgh, Joseph Black Building, Kings Buildings, West Mains Road, EH9 3FJ, Edinburgh, UK.
Coxon CR; EaStChem School of Chemistry, University of Edinburgh, Joseph Black Building, Kings Buildings, West Mains Road, EH9 3FJ, Edinburgh, UK.; Pokaż więcej
Źródło:: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Aug 01; Vol. 25 (15), pp. e202400195. Date of Electronic Publication: 2024 Jun 24.
Typ publikacji:: Journal Article; Review
MeSH Terms:: Fluorine*/chemistry
Halogenation*
Proteins*/chemistry
Proteins*/metabolism
Protein Conformation*
Nuclear Magnetic Resonance, Biomolecular*
Humans

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Tytuł:: Selective correlations between aliphatic C nuclei in protein solid-state NMR.
Autorzy:: Xiao H; National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, PR China; University of Chinese Academy of Sciences, Beijing 100049, PR China.
Zhao W; National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, PR China; Interdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology, Wuhan 430081, PR China.
Zhang Y; National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, PR China.
Kang H; National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, PR China.
Zhang Z; National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, PR China; Interdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology, Wuhan 430081, PR China. Electronic address: .
Yang J; National Center for Magnetic Resonance in Wuhan, Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, PR China; Interdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology, Wuhan 430081, PR China; Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, PR China. Electronic address: .; Pokaż więcej
Źródło:: Journal of magnetic resonance (San Diego, Calif. : 1997) [J Magn Reson] 2024 Aug; Vol. 365, pp. 107730. Date of Electronic Publication: 2024 Jul 03.
Typ publikacji:: Journal Article
MeSH Terms:: Carbon Isotopes*
Nuclear Magnetic Resonance, Biomolecular*/methods
Proteins*/chemistry
Methanosarcina/chemistry ; Algorithms

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Tytuł:: High-resolution heteronuclear correlations between spin-1/2 and half-integer quadrupolar nuclei under fast MAS solid-state NMR.
Autorzy:: Pandey MK; Indian Institute of Technology Ropar, Rupnagar, Punjab 140001, India. Electronic address: .
Nishiyama Y; JEOL Ltd., Musashino, Akishima, Tokyo 196-8558, Japan. Electronic address: .; Pokaż więcej
Źródło:: Biophysical chemistry [Biophys Chem] 2024 Jul; Vol. 310, pp. 107254. Date of Electronic Publication: 2024 May 03.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*
Quantum Theory

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Tytuł:: N backbone and methyl group resonance assignments of ricin toxin A subunit.
Autorzy:: Bhattacharya S; New York Structural Biology Center, 89 Convent Avenue, New York, NY, 10027, USA. .
Dahmane T; New York Structural Biology Center, 89 Convent Avenue, New York, NY, 10027, USA.
Goger MJ; New York Structural Biology Center, 89 Convent Avenue, New York, NY, 10027, USA.
Rudolph MJ; New York Structural Biology Center, 89 Convent Avenue, New York, NY, 10027, USA.
Tumer NE; Department of Plant Biology and Pathology, School of Environmental and Biological Sciences, Rutgers University, 59 Dudley Road, New Brunswick, NJ, 08901-8520, USA.; Pokaż więcej
Źródło:: Biomolecular NMR assignments [Biomol NMR Assign] 2024 Jun; Vol. 18 (1), pp. 85-91. Date of Electronic Publication: 2024 Apr 20.
Typ publikacji:: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms:: Ricin*/chemistry
Nuclear Magnetic Resonance, Biomolecular*
Nitrogen Isotopes*
Protein Subunits/chemistry ; Amino Acid Sequence

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Tytuł:: chemical shift-based phase modulated NMR methods for fast identification of amino acid types in proteins.
Autorzy:: Gartia J; School of Biotechnology, Kalinga Institute of Industrial Technology, Bhubaneswar, 751024, India. Electronic address: .
Barnwal RP; Department of Biophysics, Panjab University, Chandigarh, 160014, India.; Pokaż więcej
Źródło:: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Jul 05; Vol. 716, pp. 150000. Date of Electronic Publication: 2024 Apr 24.
Typ publikacji:: Journal Article
MeSH Terms:: Amino Acids*/chemistry
Nuclear Magnetic Resonance, Biomolecular*/methods
Proteins*/chemistry

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Tytuł:: Rapid Protein-Ligand Affinity Determination by Photoinduced Hyperpolarized NMR.
Autorzy:: Bütikofer M; Institute for Molecular Physical Science, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.
Stadler GR; Institute for Molecular Physical Science, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.
Kadavath H; Institute for Molecular Physical Science, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.
Cadalbert R; Institute for Molecular Physical Science, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.
Torres F; Institute for Molecular Physical Science, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.; NexMR AG, Wiesenstrasse 10A, 8952 Schlieren, Switzerland.
Riek R; Institute for Molecular Physical Science, Vladimir Prelog Weg 2, 8093 Zürich, Switzerland.; Pokaż więcej
Źródło:: Journal of the American Chemical Society [J Am Chem Soc] 2024 Jul 03; Vol. 146 (26), pp. 17974-17985. Date of Electronic Publication: 2024 Jun 18.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*
Ligands ; Protein Binding ; Photochemical Processes ; NIMA-Interacting Peptidylprolyl Isomerase/metabolism ; NIMA-Interacting Peptidylprolyl Isomerase/chemistry ; Proteins/chemistry ; Proteins/metabolism ; Peptides/chemistry ; Peptides/metabolism ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; PDZ Domains

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Tytuł:: Resolution in cryogenic solid state NMR: Challenges and solutions.
Autorzy:: Sergeyev IV; Columbia University, Department of Chemistry, New York, New York, USA.
Fritzsching K; Columbia University, Department of Chemistry, New York, New York, USA.
Rogawski R; Columbia University, Department of Chemistry, New York, New York, USA.
McDermott A; Columbia University, Department of Chemistry, New York, New York, USA.; Pokaż więcej
Źródło:: Protein science : a publication of the Protein Society [Protein Sci] 2024 Jul; Vol. 33 (7), pp. e4803.
Typ publikacji:: Journal Article; Review
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*/methods
Cold Temperature ; Proteins/chemistry ; Protein Conformation

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Tytuł:: AlphaFold2 as a replacement for solution NMR structure determination of small proteins: Not so fast!
Autorzy:: Bonin JP; Departments of Molecular Genetics and Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada; Program in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario M5G 0A4, Canada.
Aramini JM; Departments of Molecular Genetics and Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada; Program in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario M5G 0A4, Canada.
Dong Y; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Wu H; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Kay LE; Departments of Molecular Genetics and Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada; Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, Canada; Program in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, Ontario M5G 0A4, Canada. Electronic address: .; Pokaż więcej
Źródło:: Journal of magnetic resonance (San Diego, Calif. : 1997) [J Magn Reson] 2024 Jul; Vol. 364, pp. 107725. Date of Electronic Publication: 2024 Jun 19.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*/methods
Protein Folding*
Protein Conformation ; Models, Molecular ; Proteins/chemistry ; Algorithms ; Interleukin-18/chemistry ; Software

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Tytuł:: Including the Ensemble of Unstructured Conformations in the Analysis of Protein's Native State by High-Pressure NMR Spectroscopy.
Autorzy:: Berner F; Department of Chemistry, University of Konstanz, Universitätsstrasse 10, 78464, Konstanz, Germany.
Kovermann M; Department of Chemistry, University of Konstanz, Universitätsstrasse 10, 78464, Konstanz, Germany.; Pokaż więcej
Źródło:: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2024 Jul 01; Vol. 63 (27), pp. e202401343. Date of Electronic Publication: 2024 Jun 04.
Typ publikacji:: Journal Article
MeSH Terms:: Bacillus subtilis*/chemistry
Nuclear Magnetic Resonance, Biomolecular*
Bacterial Proteins*/chemistry
Pressure*
Protein Conformation*
Hydrostatic Pressure

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Tytuł:: Genetically encoded site-specific F unnatural amino acid incorporation in V. natriegens for in-cell NMR analysis.
Autorzy:: Li H; Anhui Vocational and Technical College, Hefei, Anhui, 230011, PR China; Hefei National Research Center for Interdisciplinary Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui, 230027, PR China. Electronic address: .
Zhang J; Hefei National Research Center for Interdisciplinary Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui, 230027, PR China.
Wang Z; Hefei National Research Center for Interdisciplinary Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui, 230027, PR China.
Shi P; Hefei National Research Center for Interdisciplinary Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui, 230027, PR China.
Shi C; Hefei National Research Center for Interdisciplinary Sciences at the Microscale, University of Science and Technology of China, Hefei, Anhui, 230027, PR China. Electronic address: .; Pokaż więcej
Źródło:: Protein expression and purification [Protein Expr Purif] 2024 Jul; Vol. 219, pp. 106461. Date of Electronic Publication: 2024 Mar 07.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*
Phenylalanine/chemistry ; Phenylalanine/metabolism ; Phenylalanine/genetics ; Fluorine/chemistry ; Amino Acids/chemistry ; Amino Acids/genetics ; Amino Acids/metabolism

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Tytuł:: Homonuclear Simplified Preservation of Equivalent Pathways Spectroscopy.
Autorzy:: Nimerovsky E; Department of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.
Kosteletos S; Department of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin 13125, Germany.
Lange S; Department of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin 13125, Germany.
Becker S; Department of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.
Lange A; Department of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Straße 10, Berlin 13125, Germany.
Andreas LB; Department of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.; Pokaż więcej
Źródło:: The journal of physical chemistry letters [J Phys Chem Lett] 2024 Jun 20; Vol. 15 (24), pp. 6272-6278. Date of Electronic Publication: 2024 Jun 10.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*
Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Endopeptidases/metabolism ; Endopeptidases/chemistry ; Viroporin Proteins ; Viral Matrix Proteins

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Tytuł:: Restraint validation of biomolecular structures determined by NMR in the Protein Data Bank.
Autorzy:: Baskaran K; Biological Magnetic Resonance Data Bank, Department of Molecular Biology and Biophysics, UConn Health, Farmington, CT 06030-3305, USA. Electronic address: .
Ploskon E; Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester LE1 7RH, UK.
Tejero R; Departamento de Quίmica Fίsica, Universidad de Valencia, Dr. Moliner, 50 46100 Burjassot, Valencia, Spain.
Yokochi M; Protein Data Bank Japan, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan; Protein Data Bank Japan, Protein Research Foundation, Minoh, Osaka 562-8686, Japan.
Harrus D; Protein Data Bank in Europe, EMBL-EBI, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Liang Y; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Peisach E; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Persikova I; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Ramelot TA; Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Sekharan M; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Tolchard J; Protein Data Bank in Europe, EMBL-EBI, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Westbrook JD; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Bardiaux B; Department of Structural Biology and Chemistry, Institut Pasteur, Université Paris Cité, CNRS UMR3528, 75015 Paris, France.
Schwieters CD; Computational Biomolecular Magnetic Resonance Core, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.
Patwardhan A; The Electron Microscopy Data Bank, EMBL-EBI, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Velankar S; Protein Data Bank in Europe, EMBL-EBI, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Burley SK; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Research Collaboratory for Structural Bioinformatics Protein Data Bank, San Diego Supercomputer Center, University of California, La Jolla, La Jolla, CA, USA; Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA; Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901, USA; Department of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA.
Kurisu G; Protein Data Bank Japan, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan; Protein Data Bank Japan, Protein Research Foundation, Minoh, Osaka 562-8686, Japan.
Hoch JC; Biological Magnetic Resonance Data Bank, Department of Molecular Biology and Biophysics, UConn Health, Farmington, CT 06030-3305, USA.
Montelione GT; Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, USA; Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901, USA. Electronic address: .
Vuister GW; Department of Molecular and Cell Biology, Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester LE1 7RH, UK. Electronic address: .
Young JY; Research Collaboratory for Structural Bioinformatics Protein Data Bank, Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA. Electronic address: .; Pokaż więcej
Źródło:: Structure (London, England : 1993) [Structure] 2024 Jun 06; Vol. 32 (6), pp. 824-837.e1. Date of Electronic Publication: 2024 Mar 14.
Typ publikacji:: Journal Article
MeSH Terms:: Nuclear Magnetic Resonance, Biomolecular*/methods
Databases, Protein*
Models, Molecular*
Protein Conformation*
Proteins*/chemistry
Software

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Tytuł:: Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements.
Autorzy:: Yu B; Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States.
Wang X; Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States.
Tan KN; Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States.
Iwahara J; Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States.; Pokaż więcej
Źródło:: Journal of the American Chemical Society [J Am Chem Soc] 2024 Jun 05; Vol. 146 (22), pp. 14922-14926. Date of Electronic Publication: 2024 May 21.
Typ publikacji:: Journal Article
MeSH Terms:: Static Electricity*
Nuclear Magnetic Resonance, Biomolecular*
HMGB1 Protein*/chemistry
HMGB1 Protein*/metabolism
Protein Domains*
Humans ; DNA/chemistry ; Intrinsically Disordered Proteins/chemistry ; Models, Molecular

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