Language:  

1    2  3  4  5  6  

1.  

Use of Water Proton NMR to Characterize Protein Aggregates: Gauging the Response and Sensitivity
Marc B. Taraban, Roberto A. DePaz, Brian Lobo, Yihua Bruce Yu
Analytical Chemistry, 2019, ISSN: 0003-2700, DOI: 10.1021/acs.analchem.8b05733

https://doi.org/10.1021/acs.analchem.8b05733


2.  

Effect of organic and inorganic salt environment on the complex coacervation of in situ formed protein nanoparticles and DNA
Pankaj Kumar Pandey, Priyanka Kaushik, Kamla Rawat, H. B. Bohidar
International Journal of Biological Macromolecules, 2018, ISSN: 0141-8130, DOI: 10.1016/j.ijbiomac.2018.09.088

http://www.sciencedirect.com/science/article/pii/S0141813018336936


3.  

Effect of iron oxide nanoparticles on the concentration-versus-sizes relation of proteins in the blood plasma and serum, and in model solutions
M. N. Kirichenko, N. A. Bulychev, L. L. Chaikov, M. A. Kazaryan, A. V. Masalov
XIII International Conference on Atomic and Molecular Pulsed Lasers, 2018, Volume: 10614, Pages: 106140M, DOI: 10.1117/12.2303471

https://www.spiedigitallibrary.org/conference-proceedings-of-spie/10614/106140M/Effect-of-iron-oxide-nanoparticles-on-the-concentration-versus-sizes/10.1117/12.2303471.short


4.  

Interaction of DDP with bovine serum albumin facilitates formation of the protein dimers
I. Belaya, E. Chikhirzhina, A. Polyanichko
Journal of Molecular Structure, 2017, ISSN: 0022-2860, Volume: 1140, Pages: 148-153, DOI: 10.1016/j.molstruc.2016.12.107

http://www.sciencedirect.com/science/article/pii/S0022286016314260


5.  

Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
Katerina V. Volodina, David Avnir, Vladimir V. Vinogradov
Scientific Reports, 2017, ISSN: 2045-2322, Volume: 7, DOI: 10.1038/s41598-017-01436-6

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431136/


6.  

Clusterin: full-length protein and one of its chains show opposing effects on cellular lipid accumulation
Suvarsha Rao Matukumalli, Ramakrishna Tangirala, C. M. Rao
Scientific Reports, 2017, ISSN: 2045-2322, Volume: 7, Pages: 41235, DOI: 10.1038/srep41235

http://www.nature.com/srep/2017/170125/srep41235/full/srep41235.html


7.  

Water Proton NMR: A Tool for Protein Aggregation Characterization
Marc B. Taraban, Roberto A. DePaz, Brian Lobo, Y. Bruce Yu
Analytical Chemistry, 2017, ISSN: 0003-2700, Volume: 89, Issue: 10, Pages: 5494-5502, DOI: 10.1021/acs.analchem.7b00464

http://dx.doi.org/10.1021/acs.analchem.7b00464


8.  

Interaction of Plasma Proteins with ZnSe and ZnSe@ZnS Core-Shell Quantum Dots
Irshad Ahmed Mir, Kamla Rawat, H. B. Bohidar
Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2017, ISSN: 0927-7757, DOI: 10.1016/j.colsurfa.2017.01.032

http://www.sciencedirect.com/science/article/pii/S0927775717300614


9.  

Caesalpinia bonduc serine proteinase inhibitor CbTI–2: Exploring the conformational features and antimalarial activity
Arindam Bhattacharyya, C. R. Babu
International Journal of Biological Macromolecules, 2017, ISSN: 0141-8130, DOI: 10.1016/j.ijbiomac.2017.05.044

http://www.sciencedirect.com/science/article/pii/S0141813016324436


10.  

New approach to the synthesis of a functional macroporous poly(vinyl alcohol) network and design of boronate affinity sorbent for protein separation
Vladimir E. Tikhonov, Inesa V. Blagodatskikh, Vladimir A. Postnikov, Zinaida S. Klemenkova, Oxana V. Vyshivannaya, Alexei R. Khokhlov
European Polymer Journal, 2016, ISSN: 0014-3057, Volume: 75, Pages: 1-12, DOI: 10.1016/j.eurpolymj.2015.11.035

http://www.sciencedirect.com/science/article/pii/S0014305715300768


1    2  3  4  5  6