Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Daniel S. Spencer"'
Publikováno v:
Biophysical Chemistry. :86-94
Six single substitution mutations, V66F, V66G, V66N, V66Q, V66S, V66T, and V66Y, were made in the background of a highly stable triple mutant (P117G, H124L, and S128A) of staphylococcal nuclease. The thermodynamic stabilities of wild type staphylococ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fed08de79e5e08e67e0ac866cd79bef
https://doi.org/10.1016/j.bpc.2013.06.018
https://doi.org/10.1016/j.bpc.2013.06.018
Autor:
Daniel A. Karp, Wesley E. Stites, Apostolos G. Gittis, John J. Dwyer, Daniel S. Spencer, Eaton E. Lattman, E Bertrand García-Moreno
Publikováno v:
ResearcherID
A glutamic acid was buried in the hydrophobic core of staphylococcal nuclease by replacement of Val-66. Its pK(a) was measured with equilibrium thermodynamic methods. It was 4.3 units higher than the pK(a) of Glu in water. This increase was comparabl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2f68def1c065232b93ae83aa2637047
Autor:
Wesley E. Stites, Apostolos G. Gittis, John J. Dwyer, Bertrand Garcia-Moreno, Eaton E. Lattman, Daniel S. Spencer
Publikováno v:
Biophysical Chemistry. 64:211-224
The dielectric inside a protein is a key physical determinant of the magnitude of electrostatic interactions in proteins. We have measured this dielectric phenomenologically, in terms of the dielectric that needs to be used with the Born equation in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7bac76872bd71ccaa594acb88356440
https://doi.org/10.1016/s0301-4622(96)02238-7
https://doi.org/10.1016/s0301-4622(96)02238-7
Publikováno v:
Journal of molecular biology. 351(1)
Environmental variables can exert significant influences on the folding stability of a protein, and elucidating these influences provides insight on the determinants of protein stability. Here, experimental data on the stability of FKBP12 are reporte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a75305bd7a4560c56c0337f3e905d6f
https://pubmed.ncbi.nlm.nih.gov/15992823
https://pubmed.ncbi.nlm.nih.gov/15992823
Autor:
Daniel S. Spencer, Junmei Chen, Michael P. Byrne, Jason B. Holder, Wesley E. Stites, Allen F. Bennett
Publikováno v:
Biochemistry. 40(46)
To examine the importance of side chain packing to protein stability, each of the 11 leucines in staphylococcal nuclease was substituted with isoleucine and valine. The nine valines were substituted with leucine and isoleucine, while the five isoleuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::855462a258ef92865da4f4a833f6c1a2
https://pubmed.ncbi.nlm.nih.gov/11705391
https://pubmed.ncbi.nlm.nih.gov/11705391
Publikováno v:
Protein engineering. 14(5)
The biological activity of some proteins is known to be sensitive to oxidative damage caused by a variety of oxidants. The model protein staphylococcal nuclease was used to explore the effect on protein structural stability of oxidizing methionine to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06fc716f4d23951e25ceaafb8c8fa87d
https://pubmed.ncbi.nlm.nih.gov/11438757
https://pubmed.ncbi.nlm.nih.gov/11438757
Autor:
Daniel S. Spencer, Wesley E. Stites
Publikováno v:
Journal of molecular biology. 257(3)
The M32L substitution mutation of staphylococcal nuclease was made to test the theoretical prediction by Yamaotsu, Moriguchi and Hirono that it would be approximately 1.6 kcal/mol more stable than the wild-type protein. Instead M32L and the closely r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d7e551e6de3e7882f1809f04db8da76
https://pubmed.ncbi.nlm.nih.gov/8648619
https://pubmed.ncbi.nlm.nih.gov/8648619