Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Gerald R, Grimsley"'
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
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
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:
Journal of Molecular Biology. 362:594-604
The ionizable groups in proteins with the lowest pKs are the carboxyl groups of aspartic acid side-chains. One of the lowest, pK=0.6, is observed for Asp76 in ribonuclease T1. This low pK appeared to result from hydrogen bonds to a water molecule and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::215b9b747f20acb829a1d81209b6db9f
https://doi.org/10.1016/j.jmb.2006.07.056
https://doi.org/10.1016/j.jmb.2006.07.056
Publikováno v:
Protein Science. 15:1214-1218
We have used potentiometric titrations to measure the pK values of the ionizable groups of proteins in alanine pentapeptides with appropriately blocked termini. These pentapeptides provide an improved model for the pK values of the ionizable groups i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71c5ab2712d47e9b8d6b78b1cd9f268f
https://doi.org/10.1110/ps.051840806
https://doi.org/10.1110/ps.051840806
Autor:
James M. Briggs, Beatrice M. P. Huyghues-Despointes, J. Martin Scholtz, C. Nick Pace, Gerald R. Grimsley
Publikováno v:
Biophysical Chemistry. :211-219
Coulomb's law and a finite difference Poisson-Boltzmann based analysis are used to predict the pK values for 15 ionizable side chains (6 Asp, 6 Glu and 3 His) in ribonuclease T1. These predicted values are compared to the measured pK values to gain i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0147a2cf5fe9f4e4e864ae999bdfea3d
https://doi.org/10.1016/s0301-4622(02)00192-8
https://doi.org/10.1016/s0301-4622(02)00192-8