Zobrazeno 1 - 10
of 94
pro vyhledávání: '"J Martin Scholtz"'
Publikováno v:
FEBS Letters. 588:2177-2184
The goal of this article is to summarize what has been learned about the major forces stabilizing proteins since the late 1980s when site-directed mutagenesis became possible. The following conclusions are derived from experimental studies of hydroph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d0449b80132e577ff62742dad4bdf19
https://doi.org/10.1016/j.febslet.2014.05.006
https://doi.org/10.1016/j.febslet.2014.05.006
Autor:
Lubica Urbanikova, Satoshi Imura, John Landua, J. Martin Scholtz, Bret A. Shirley, C. Nick Pace, D Schell, Saul R. Trevino, Gerald R. Grimsley, Hailong Fu, Jozef Sevcik, Richard L. Thurlkill, Eric J. Hebert, Kazufumi Takano, Ketan S. Gajiwala, Jeffery K. Myers, Katrina Lee Fryar
Publikováno v:
Protein Science. 23:652-661
Our goal was to gain a better understanding of the contribution of the burial of polar groups and their hydrogen bonds to the conformational stability of proteins. We measured the change in stability, Δ(ΔG), for a series of hydrogen bonding mutants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1256f62f93690feba03e44988085071
https://doi.org/10.1002/pro.2449
https://doi.org/10.1002/pro.2449
Publikováno v:
Biophysical Journal. 102:1907-1915
Protein solubility is a problem for many protein chemists, including structural biologists and developers of protein pharmaceuticals. Knowledge about how intrinsic factors influence solubility is limited due to the difficulty of obtaining quantitativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4b137521a8c383488ac6e5e7267e2e9
https://doi.org/10.1016/j.bpj.2012.01.060
https://doi.org/10.1016/j.bpj.2012.01.060
Autor:
Hailong Fu, J. Martin Scholtz, Bret A. Shirley, John Landua, Saul R. Trevino, Marsha McNutt Hendricks, Gerald R. Grimsley, Katrina Lee Fryar, Satoshi Iimura, C. Nick Pace, Ketan S. Gajiwala
Publikováno v:
Journal of Molecular Biology. 408:514-528
Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1062f4963b9c6e2b650b279cce36c197
https://doi.org/10.1016/j.jmb.2011.02.053
https://doi.org/10.1016/j.jmb.2011.02.053
Publikováno v:
Protein Science. 19:1044-1052
Increasing the conformational stability of proteins is an important goal for both basic research and industrial applications. In vitro selection has been used successfully to increase protein stability, but more often site-directed mutagenesis is use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e80ae96e77b438a6271478290db74ee
https://doi.org/10.1002/pro.381
https://doi.org/10.1002/pro.381
Autor:
J. Martin Scholtz, Gerald R. Grimsley, C. Nick Pace, Beatrice M. P. Huyghues-Despointes, Hailong Fu, Kazufumi Takano
Publikováno v:
Protein Science. 19:929-943
The goal of this article is to gain a better understanding of the denatured state ensemble (DSE) of proteins through an experimental and computational study of their denaturation by urea. Proteins unfold to different extents in urea and the most hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3dba713175b8279e8939899aa6f5c52e
https://doi.org/10.1002/pro.370
https://doi.org/10.1002/pro.370
Autor:
J. Martin Scholtz, David H. Russell, C. Nick Pace, Zhaoxiang Wu, John A. McLean, Christopher Becker, Lisa M. Pérez, Janel R. McLean
Publikováno v:
The Journal of Physical Chemistry B. 114:809-816
Ion mobility-mass spectrometry is used to investigate the structure(s) of a series of model peptide [M + H](+) ions to better understand how intrinsic properties affect structure in low dielectric environments. The influence of peptide length, amino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10990f68a406fc2df07667a4d93246e7
https://doi.org/10.1021/jp9105103
https://doi.org/10.1021/jp9105103
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 77:491-498
Our goal was to gain a better understanding of how protein stability can be increased by improving β-turns. We studied 22 β-turns in nine proteins with 66 to 370 residues by replacing other residues with proline and glycine and measuring the stabil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79c9ac5d3fcf3b998600d0fb9852538f
https://doi.org/10.1002/prot.22509
https://doi.org/10.1002/prot.22509
Publikováno v:
Protein Science. 12:2374-2378
Ribonuclease Sa and two charge-reversal variants can be converted into amyloid in vitro by the addition of 2,2,2-triflouroethanol (TFE). We report here amyloid fibril formation for these proteins as a function of pH. The pH at maximal fibril formatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78ba7412b06690130837d00a1c8144da
https://doi.org/10.1110/ps.03152903
https://doi.org/10.1110/ps.03152903
Publikováno v:
Journal of Pharmaceutical Sciences. 97:4155-4166
High concentration protein delivery is difficult to achieve for several protein pharmaceuticals due to low solubility. In this review, we discuss different types of low protein solubility, including low in vitro solubility, which is relevant to the f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22f7b9dadc1c154ab4df22dceba0da3e
https://doi.org/10.1002/jps.21327
https://doi.org/10.1002/jps.21327