Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Roy W. Alston"'
Publikováno v:
Analytical Biochemistry. 437:185-197
A simultaneous multiple sample light scattering (SMSLS) prototype instrument was built to simultaneously measure light scattering from many independent monoclonal antibody (mAb) solutions in order to monitor their time-dependent aggregation behavior
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b221e7abda7636ab0d39335474dc41de
https://doi.org/10.1016/j.ab.2013.02.014
https://doi.org/10.1016/j.ab.2013.02.014
Autor:
Shujun Bai, Lantz Steven Andrew, Tia Estey, Maloney Kevin, Pavel Landsman, Karin Lucas, Mark L. Brader, Roy W. Alston
Publikováno v:
Molecular pharmaceutics. 12(4)
Screening for pharmaceutically viable stability from measurements of thermally induced protein unfolding and short-term accelerated stress underpins much molecule design, selection, and formulation in the pharmaceutical biotechnology industry. Howeve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a44d01b0ef3897cbcb7f54a489694fa
https://pubmed.ncbi.nlm.nih.gov/25687223
https://pubmed.ncbi.nlm.nih.gov/25687223
Publikováno v:
Protein Science. 9:1395-1398
Several recent studies have shown that it is possible to increase protein stability by improving electrostatic interactions among charged groups on the surface of the folded protein. However, the stability increases are considerably smaller than pred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7e1d85b11257a6340a6f2d423f2f7ea
https://doi.org/10.1110/ps.9.7.1395
https://doi.org/10.1110/ps.9.7.1395
Autor:
Gerald R. Grimsley, Mauricio Lasagna, J. Martin Scholtz, C. Nick Pace, Gregory D. Reinhart, Roy W. Alston
Publikováno v:
Biophysical journal. 94(6)
This article probes the denatured state ensemble of ribonuclease Sa (RNase Sa) using fluorescence. To interpret the results obtained with RNase Sa, it is essential that we gain a better understanding of the fluorescence properties of tryptophan (Trp)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdcdf72fa5878f08cda39343b67c5618
https://pubmed.ncbi.nlm.nih.gov/18065477
https://pubmed.ncbi.nlm.nih.gov/18065477
Autor:
Gregory D. Reinhart, Mauricio Lasagna, J. Martin Scholtz, Lubica Urbanikova, Jozef Sevcik, Roy W. Alston, C. Nick Pace
Publikováno v:
Biophysical journal. 87(6)
Ribonuclease Sa (RNase Sa) contains no tryptophan (Trp) residues. We have added single Trp residues to RNase Sa at sites where Trp is found in four other microbial ribonucleases, yielding the following variants of RNase Sa: Y52W, Y55W, T76W, and Y81W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::747c81923f3f84313e0dfbb8107adce0
https://pubmed.ncbi.nlm.nih.gov/15377518
https://pubmed.ncbi.nlm.nih.gov/15377518
Autor:
J. M. Scholtz, Gerald R. Grimsley, Beatrice M. P. Huyghues-Despointes, L. R. Fee, Roy W. Alston, Pace Cn, Richard L. Thurlkill, Kevin L. Shaw
Publikováno v:
Protein science : a publication of the Protein Society. 8(9)
It is difficult to increase protein stability by adding hydrogen bonds or burying nonpolar surface. The results described here show that reversing the charge on a side chain on the surface of a protein is a useful way of increasing stability. Ribonuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67ef9b86e71629e34eb90662f0f78248
https://pubmed.ncbi.nlm.nih.gov/10493585
https://pubmed.ncbi.nlm.nih.gov/10493585
Autor:
C. Nick Pace, Gerald R. Grimsley, J. Martin Scholtz, Roy W. Alston, Gregory D. Reinhart, Mauricio Lasagna
Publikováno v:
Biophysical Journal. (6):2288-2296
Characterizing the denatured state ensemble is crucial to understanding protein stability and the mechanism of protein folding. The aim of this research was to see if fluorescence could be used to gain new information on the denatured state ensemble.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::641dbfa29045dd4966ba0f5721473afc