Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Beatrice M. P. Huyghues-Despointes"'
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:
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
Publikováno v:
Protein Science. 2:1604-1611
A single aspartate residue has been placed at various positions in individual peptides for which the alanine-based reference peptide is electrically neutral, and the helix contents of the peptides have been measured by circular dichroism. The depende
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eceac8c0e1d5094b34c3cec772b408bb
https://doi.org/10.1002/pro.5560021006
https://doi.org/10.1002/pro.5560021006
Publikováno v:
Protein Science. 2:80-85
The helix-stabilizing effects of repeating pairs of Asp-Arg and Glu-Arg residues have been characterized using a peptide system of the same design used earlier to study Glu-Lys (Marqusee, S. & Baldwin, R.L., 1987, Proc. Natl. Acad. Sci. USA 84, 8898-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dba3d9d74576b80d4b48edc43bb40d4b
https://doi.org/10.1002/pro.5560020108
https://doi.org/10.1002/pro.5560020108
Publikováno v:
Biochemistry. 31:1476-1483
Apamin is an 18-residue bee venom peptide with the sequence CNCKAPETALCARRCQQH-amide and contains 2 disulfide bonds connecting C-1 to C-11 and C-3 to C-15. In the folding of reduced, unfolded apamin to native apamin with two disulfide bonds, the one-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::405cd57fd80f5f2c9bbee5807ff3de02
https://doi.org/10.1021/bi00120a026
https://doi.org/10.1021/bi00120a026
Publikováno v:
Proteins. 69(2)
The stability and structure of several beta-hairpin peptide variants derived from the C-terminus of the B1 domain of protein G were investigated by a number of experimental and computational techniques. Our analysis shows that the structure and stabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23727701123a561a728b113c1389a7bf
https://pubmed.ncbi.nlm.nih.gov/17600831
https://pubmed.ncbi.nlm.nih.gov/17600831
Autor:
J. Martin Scholtz, Aiping Zhu, Liviu Movileanu, Dmitrii E. Makarov, Serdal Kirmizialtin, Carl P. Goodrich, Beatrice M. P. Huyghues-Despointes
Publikováno v:
The journal of physical chemistry. B. 111(13)
We used single-channel electrical recordings and Langevin molecular dynamics simulations to explore the electrophoretic translocation of various beta-hairpin peptides across the staphylococcal alpha-hemolysin (alphaHL) protein pore at single-molecule
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da86220b34af52bffb7243a5a97eca1b
https://pubmed.ncbi.nlm.nih.gov/17388500
https://pubmed.ncbi.nlm.nih.gov/17388500
Autor:
C. Nick Pace, D Schell, James M. Briggs, Stephanie Newsom, Richard L. Thurlkill, Saul R. Trevino, Marta Bruix, Gerald R. Grimsley, Jan M. Antosiewicz, Kevin L. Shaw, Beatrice M. P. Huyghues-Despointes, Douglas V. Laurents, J. Martin Scholtz, Manuel Rico
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
The pK values of the titratable groups in ribonuclease Sa (RNase Sa) (pI=3.5), and a charge-reversed variant with five carboxyl to lysine substitutions, 5K RNase Sa (pI=10.2), have been determined by NMR at 20 °C in 0.1 M NaCl. In RNase Sa, 18 pK va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13a612153c6170583190e7e3e5a5f02a
http://hdl.handle.net/10261/257802
http://hdl.handle.net/10261/257802
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
Hydrogen-exchange rates were measured for RNase T1 and three variants with Ala --> Gly substitutions at a solvent-exposed (residue 21) and a buried (residue 23) position in the helix: A21G, G23A, and A21G + G23A. These results were used to measure th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f2ecf3974c42904e83b9900b8305e65
https://biblio.vub.ac.be/vubir/hydrogenexchange-stabilities-of-rnase-t1-and-variants-with-buried-and-solventexposed-ala-gly-mutations-in-the-helix(5687f73b-4a81-42d6-b72c-1f696f7dab56).html
https://biblio.vub.ac.be/vubir/hydrogenexchange-stabilities-of-rnase-t1-and-variants-with-buried-and-solventexposed-ala-gly-mutations-in-the-helix(5687f73b-4a81-42d6-b72c-1f696f7dab56).html