Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Guillermo A, Bermejo"'
Publikováno v:
Angew Chem Int Ed Engl
Glutamine-binding protein (GlnBP) from Escherichia coli is a prototypical periplasmic binding protein that has been crystallized in an apo, “open” conformation, with its two domains far apart, and a holo, “closed” form, with proximal domains
Publikováno v:
Protein Sci
We introduce a new hydrogen bonding potential of mean force generated from high-quality crystal structures for use in Xplor-NIH structure calculations. This term applies to hydrogen bonds involving both backbone and sidechain atoms. When used in stru
Autor:
Nico Tjandra, Rohith Rajasekaran, Jan Marchant, Guillermo A. Bermejo, Madeleine Strickland, Colin T. O’Hern, Michael F. Summers, Jonathan Catazaro, Marie-Paule Strub
Publikováno v:
Journal of the American Chemical Society. 141:1430-1434
NMR has provided a wealth of structural and dynamical information for RNA molecules of up to ∼50 nucleotides, but its application to larger RNAs has been hampered in part by difficulties establishing global structural features. A potential solution
Autor:
Amber L H, Gray, Carlos A, Steren, Isaac W, Haynes, Guillermo A, Bermejo, Filippo, Favretto, Markus, Zweckstetter, Thanh D, Do
Publikováno v:
The journal of physical chemistry. B. 125(5)
Falling outside of Lipinski's rule of five, macrocyclic drugs have accessed unique binding sites of their target receptors unreachable by traditional small molecules. Cyclosporin(e) A (CycA), an extensively studied macrocyclic natural product, is an
Autor:
Filippo Favretto, Markus Zweckstetter, Isaac W. Haynes, Carlos A. Steren, Guillermo A. Bermejo, Thanh D. Do, Amber L. H. Gray
Publikováno v:
The journal of physical chemistry / B 125(5), 1378-1391 (2021). doi:10.1021/acs.jpcb.0c11152
Falling outside of Lipinski's rule of five, macrocyclic drugs have accessed unique binding sites of their target receptors unreachable by traditional small molecules. Cyclosporin(e) A (CycA), an extensively studied macrocyclic natural product, is an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::752de8a345657c0f46c282f3b36a2f75
Publikováno v:
Protein Science. 27:26-40
Xplor-NIH is a popular software package for biomolecular structure determination from nuclear magnetic resonance (NMR) and other data sources. Here, some of Xplor-NIH's most useful data-associated energy terms are reviewed, including newer alternativ
Publikováno v:
Methods in Molecular Biology ISBN: 9781493973859
Xplor-NIH is a popular software package for biomolecular structure determination from NMR (and other) experimental data. This chapter illustrates its use with the de novo structure determination of the B1 domain of streptococcal protein G (GB1), base
Autor:
Richard J. Youle, Kristi L. Norris, Junhe Ma, Guillermo A. Bermejo, Nico Tjandra, Frank Edlich
Publikováno v:
Proceedings of the National Academy of Sciences. 109:20901-20906
The human protein Bax sits at a critical regulatory junction of apoptosis, or programmed cell death. Bax exists in equilibrium between cytosolic and mitochondria-associated forms that shifts toward the latter when Bax is activated by proapoptotic pro
Publikováno v:
Protein Science. 21:1824-1836
Statistical potentials that embody torsion angle probability densities in databases of high-quality X-ray protein structures supplement the incomplete structural information of experimental nuclear magnetic resonance (NMR) datasets. By biasing the co
Here, we show that modern solution nuclear magnetic resonance (NMR) structures of RNA exhibit more steric clashes and conformational ambiguities than their crystallographic X-ray counterparts. To tackle these issues, we developed RNA-ff1, a new force
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9fc016cdfd24cf6d762adff17bb6350
https://europepmc.org/articles/PMC4856558/
https://europepmc.org/articles/PMC4856558/