Výsledky vyhledávání - "G.V.T. Swapna"

Structure Determination of Challenging Protein–Peptide Complexes Combining NMR Chemical Shift Data and Molecular Dynamics Simulations

Autor: Arup Mondal, G.V.T. Swapna, Maria M. Lopez, Laura Klang, Jingzhou Hao, LiChung Ma, Monica J. Roth, Gaetano T. Montelione, Alberto Perez

Publikováno v: J Chem Inf Model

Intrinsically disordered regions of proteins often mediate important protein–protein interactions. However, the folding-upon-binding nature of many polypeptide–protein interactions limits the ability of modeling tools to predict the three-dimensi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2896313d0e69f68fd897e44cc63cc0a1
https://doi.org/10.1021/acs.jcim.2c01595

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SpecDB: A relational database for archiving biomolecular NMR spectral data

Autor: Keith J. Fraga, Yuanpeng J. Huang, Theresa A. Ramelot, G.V.T. Swapna, Arwin Lashawn Anak Kendary, Ethan Li, Ian Korf, Gaetano T. Montelione

Publikováno v: J Magn Reson

NMR is a valuable experimental tool in the structural biologist's toolkit to elucidate the structures, functions, and motions of biomolecules. The progress of machine learning, particularly in structural biology, reveals the critical importance of la

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2581f7d857ed640909e0263b24da27c4
https://escholarship.org/uc/item/9z15792m

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Akademický článek

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Structure determination of protein-peptide complexes from NMR chemical shift data using MELD

Autor: Arup Mondal, G.V.T. Swapna, Jingzhou Hao, LiChung Ma, Monica J. Roth, Gaetano T. Montelione, Alberto Perez

Intrinsically disordered regions of proteins often mediate important protein-protein interactions. However, the folding upon binding nature of many polypeptide-protein interactions limits the ability of modeling tools to predict structures of such co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::437c1f879b5a5633d2bcd6fb1babd36c
https://doi.org/10.1101/2021.12.31.474671

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Solution NMR structure of Lin0431 protein from Listeria innocua reveals high structural similarity with domain II of bacterial transcription antitermination protein NusG

Autor: Yuefeng Tang, G.V.T. Swapna, Burkhard Rost, Gaetano T. Montelione, Thomas Acton, Haleema Janjua, John K. Everett, D. Lee, Colleen Ciccosanti, Rong Xiao

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 78:2563-2568

Lin0431 protein from Listeria innocua (UniProtKB/TrEMBL ID {"type":"entrez-protein","attrs":{"text":"Q92EM7","term_id":"81527521","term_text":"Q92EM7"}}Q92EM7/Q92EM7_LISIN) was selected as a target of the Northeast Structural Genomics Consortium (tar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::768a220044c0e638fe91577dd4f45f90
https://doi.org/10.1002/prot.22760

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Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A

Autor: Darmawi Juminaga, G.V.T. Swapna, Gaetano T. Montelione, Harold A. Scheraga, William J. Wedemeyer, Ying Xiong

Publikováno v: Protein Science. 9:421-426

Proline peptide group isomerization can result in kinetic barriers in protein folding. In particular, the cis proline peptide conformation at Tyr92-Pro93 of bovine pancreatic ribonuclease A (RNase A) has been proposed to be crucial for chain folding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6452c5bd3c79c75265136fa72b401e09
https://doi.org/10.1110/ps.9.2.421

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Comparisons of NMR Spectral Quality and Success in Crystallization Demonstrate that NMR and X-ray Crystallography Are Complementary Methods for Small Protein Structure Determination

Autor: Rong Xiao, Thomas Acton, Jinfeng Liu, Philip C. Manor, M. Ciano, B. Rost, Gaetano T. Montelione, Paolo Rossi, Yang Chen, G.V.T. Swapna, P. A. Rajan, John P. Hunt, James M. Aramini, Natalia G. Denissova, David A. Snyder, Richard Karlin

Publikováno v: Journal of the American Chemical Society. 127:16505-16511

X-ray crystallography and NMR spectroscopy provide the only sources of experimental data from which protein structures can be analyzed at high or even atomic resolution. The degree to which these methods complement each other as sources of structural

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b193000b77f6a4e7e133f13393044f6
https://doi.org/10.1021/ja053564h

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Akademický článek

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Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle α-tropomyosin in an engineered chimeric protein 1 1Edited by P. E. Wright

Autor: Thomas Palm, G.V.T. Swapna, Gaetano T. Montelione, Norma J. Greenfield, Yuanpeng J. Huang, Daniel Monleon, Sarah E. Hitchcock-DeGregori

Publikováno v: Journal of Molecular Biology. 312:833-847

Tropomyosin is an alpha-helical coiled-coil protein that aligns head-to-tail along the length of the actin filament and regulates its function. The solution structure of the functionally important N terminus of a short 247-residue non-muscle tropomyo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d8486fa6cf1be4f2feb39462a9722ab0
https://doi.org/10.1006/jmbi.2001.4982

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