Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Christine Jorge"'
Autor:
Martins S. Oderinde, Soomin Jin, Jayanta Das, Christine Jorge, Shiuhang Yip, Antonio Ramirez, Dauh-Rurng Wu, Ying Li, James Kempson, Nicholas A. Meanwell, Arvind Mathur, T. G. Murali Dhar
Publikováno v:
ACS Catalysis. 12:12511-12520
Autor:
Joseph Pawluczyk, Nicholas A. Meanwell, Muthalagu Vetrichelvan, Arvind Mathur, T. G. Murali Dhar, Manivel Pitchai, James Kempson, Cornelius Lyndon A M, Martins S. Oderinde, Arun Kumar Gupta, Antonio Ramirez, Edna Mao, Christine Jorge, Anuradha Gupta
Publikováno v:
Journal of the American Chemical Society. 142:3094-3103
We describe the synthesis through visible-light photocatalysis of novel functionalized tetracyclic scaffolds that incorporate a fused azabicyclo[3.2.0]heptan-2-one motif, which are structurally interesting cores with potential in natural product synt
Autor:
Amy A. Sarjeant, Arvind Mathur, Cornelius Lyndon A M, Christine Jorge, Nicholas A. Meanwell, James Kempson, T. G. Murali Dhar, Joseph Pawluczyk, Bhupinder Sandhu, Antonio Ramirez, Martins S. Oderinde, Darpandeep Aulakh
Publikováno v:
The Journal of organic chemistry. 86(2)
Indole and indoline rings are important pharmacophoric scaffolds found in marketed drugs, agrochemicals, and biologically active molecules. The [2 + 2] cycloaddition reaction is a versatile strategy for constructing architecturally interesting, sp3-r
Autor:
A. Joshua Wand, Nathaniel V. Nucci, Matthew A. Stetz, Kathleen G. Valentine, Bryan S. Marques, Christine Jorge
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-8 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-8 (2020)
Conformational entropy can be an important element of the thermodynamics of protein functions such as the binding of ligands. The observed role for conformational entropy in modulating molecular recognition by proteins is in opposition to an often-in
Autor:
A. Joshua Wand, Brian Fuglestad, Bryan S. Marques, Nicole E. Kerstetter, Kathleen G. Valentine, Christine Jorge
Publikováno v:
Methods in enzymology. 615
Reverse micelle (RM) encapsulation of proteins for NMR spectroscopy has many advantages over standard NMR methods such as enhanced tumbling and improved sensitivity. It has opened many otherwise difficult lines of investigation including the study of
Protein hydration is a critical aspect of protein stability, folding, and function and yet remains difficult to characterize experimentally. Solution NMR offers a route to a site-resolved view of the dynamics of protein-water interactions through the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39b355ee7866e040c122e6fee5920f53
https://doi.org/10.1016/bs.mie.2018.09.040
https://doi.org/10.1016/bs.mie.2018.09.040
Autor:
A. Joshua Wand, Christine Jorge, Evangelia A. Athanasoula, Kristina W. C. Wang, Nathaniel V. Nucci, Bryan S. Marques, Igor Dodevski
Publikováno v:
The Journal of Physical Chemistry. B
The encapsulation of proteins and nucleic acids within the nanoscale water core of reverse micelles has been used for over 3 decades as a vehicle for a wide range of investigations including enzymology, the physical chemistry of confined spaces, prot
Autor:
Starla D. Glover, Cecilia Tommos, Li Liang, Kathleen G. Valentine, Christine Jorge, Leif Hammarström
Publikováno v:
Journal of the American Chemical Society
Tyrosine oxidation-reduction involves proton-coupled electron transfer (PCET) and a reactive radical state. These properties are effectively controlled in enzymes that use tyrosine as a high-potential, one-electron redox cofactor. The α3Y model prot
Autor:
A. Joshua Wand, Christine Jorge, Nathaniel V. Nucci, Bertrand Garcia-Moreno, Gurnimrat K. Sidhu
Publikováno v:
Biophysical Journal. 104(2)
Measurements of water dynamics and protein-water interactions are essential to understanding protein folding, structure, function, and dynamics. However, protein-water interactions have historically been difficult to study and have mostly been limite
Autor:
Bryan S. Marques, A. Joshua Wand, Christine Jorge, Bertrand Garcia-Moreno, Nathaniel V. Nucci
Publikováno v:
Biophysical Journal. 108:48a
The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Protein hydration has historically been quite difficult to measure experimentally. Confinement of a solvated protein within the protec