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Large-Scale Refinement of Metal−Organic Framework Structures Using Density Functional Theory
Nazarian, Dalar,Camp, Jeffrey S.,Chung, Yongchul G.,Snurr, Randall Q.,Sholl, David S. American Chemical Society 2017 Chemistry of materials Vol.29 No.6
<P>Efforts to computationally characterize large numbers of nanoporous materials often rely on databases of experimentally resolved crystal structures. The accuracy of experimental crystal structures used in such calculations has a significant impact on the reliability of the results. In this work, we report structures optimized using periodic density functional theory (DFT) for more than 800 experimentally synthesized metal-organic frameworks (MOFs). Many MOFs changed significantly upon structural optimization, particularly materials that were crystallographically resolved in their solvated form. For each MOF, we simulated the adsorption of CH4 and CO2 using grand canonical Monte Carlo both before and after DFT optimization. The DFT optimization has a large impact on simulated gas adsorption in some cases. For example, CO2 loading at 1 bar changed by more than 25% in over 25% of the MOFs we considered.</P>
Bio-Frontier Symposia : Proteomics ; Advanced strategies for protein profiling using LC-FTICR/MS
( Ljiljana Pasa Toli ),( Gordon A. Anderson ),( Mary S. Lipton ),( David G. Camp II ),( Yu Feng Shen ),( Christophe Masselon ),( Richard D. Smith ) 한국생화학분자생물학회 (구 한국생화학회) 2005 62회 KSBMB Annual Meeting in 2005 Vol.- No.-
Bio-Frontier Symposia : Proteomics ; Advanced strategies for protein profiling using LC-FTICR/MS
( Ljiljana Pasa Tolic ),( Gordon A. Anderson ),( Mary S. Lipton ),( David G. Camp ),( Yu Feng Shen ),( Christophe Masselon ),( Richard D. Smith ) 한국생화학분자생물학회 (구 한국생화학회) 2005 생화학분자생물학회 춘계학술발표논문집 Vol.2005 No.-
Highly stable trypsin-aggregate coatings on polymer nanofibers for repeated protein digestion
Kim, Byoung Chan,Lopez-Ferrer, Daniel,Lee, Sang-Mok,Ahn, Hye-Kyung,Nair, Sujith,Kim, Seong H.,Kim, Beom Soo,Petritis, Konstantinos,Camp, David G.,Grate, Jay W.,Smith, Richard D.,Koo, Yoon-Mo,Gu, Man B WILEY-VCH Verlag 2009 Proteomics Vol.9 No.7
<P>A stable and robust trypsin-based biocatalytic system was developed and demonstrated for proteomic applications. The system utilizes polymer nanofibers coated with trypsin aggregates for immobilized protease digestions. After covalently attaching an initial layer of trypsin to the polymer nanofibers, highly concentrated trypsin molecules are crosslinked to the layered trypsin by way of a glutaraldehyde treatment. This process produced a 300-fold increase in trypsin activity compared with a conventional method for covalent trypsin immobilization, and proved to be robust in that it still maintained a high level of activity after a year of repeated recycling. This highly stable form of immobilized trypsin was resistant to autolysis, enabling repeated digestions of BSA over 40 days and successful peptide identification by LC-MS/MS. This active and stable form of immobilized trypsin was successfully employed in the digestion of yeast proteome extract with high reproducibility and within shorter time than conventional protein digestion using solution phase trypsin. Finally, the immobilized trypsin was resistant to proteolysis when exposed to other enzymes (i.e., chymotrypsin), which makes it suitable for use in “real-world” proteomic applications. Overall, the biocatalytic nanofibers with trypsin aggregate coatings proved to be an effective approach for repeated and automated protein digestion in proteomic analyses.</P>