Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Carolyn A. Fitch"'
Publikováno v:
Biophysical Journal. 120:89a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f65ad860ab69eb3b0c8de79c803fe92
https://doi.org/10.1016/j.bpj.2020.11.746
https://doi.org/10.1016/j.bpj.2020.11.746
Publikováno v:
Protein Science. 24:752-761
Using complementary approaches of potentiometry and NMR spectroscopy, we have determined that the equilibrium acid dissociation constant (pKa value) of the arginine guanidinium group is 13.8 ± 0.1. This is substantially higher than that of ∼ 12 of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27cc73d57295e132ac09e9dcf95ba896
https://doi.org/10.1002/pro.2647
https://doi.org/10.1002/pro.2647
Autor:
Jamie L. Schlessman, Carlos A. Castañeda, Carolyn A. Fitch, Ananya Majumdar, V.S. Khangulov, Bertrand Garcia-Moreno
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 77:570-588
Prior computational studies of the acid-unfolding behavior of staphylococcal nuclease (SNase) suggest that the pKa values of its carboxylic groups are difficult to reproduce with electrostatics calculations with continuum methods. To examine the mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ded8a921a7c651bfcc0f2c9f10e03ea8
https://doi.org/10.1002/prot.22470
https://doi.org/10.1002/prot.22470
Autor:
Jamie L. Schlessman, Ana Damjanović, Carolyn A. Fitch, Angel E. Garcia, E Bertrand García-Moreno
Publikováno v:
Biophysical Journal. 93:2791-2804
Molecular dynamics simulations of Staphylococcal nuclease and of 10 variants with internal polar or ionizable groups were performed to investigate systematically the molecular determinants of hydration of internal cavities and pockets in proteins. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa32bb023bb33e646d7d8f9ceff7033c
https://doi.org/10.1529/biophysj.107.104182
https://doi.org/10.1529/biophysj.107.104182
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 63:113-126
The acid unfolding of staphylococcal nuclease (SNase) is very cooperative (Whitten and García-Moreno, Biochemistry 2000;39:14292-14304). As many as seven hydrogen ions (H+) are bound preferentially by the acid-unfolded state relative to the native (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb22e077a888255d4237dc1ada866633
https://doi.org/10.1002/prot.20797
https://doi.org/10.1002/prot.20797
Autor:
E Bertrand García-Moreno, Daniel A. Karp, Carolyn A. Fitch, Wesley E. Stites, Eaton E. Lattman, Kelly K. Lee
Publikováno v:
ResearcherID
Lys-66 and Glu-66, buried in the hydrophobic interior of staphylococcal nuclease by mutagenesis, titrate with pK a values of 5.7 and 8.8, respectively (Dwyer et al., 2000, Biophys. J. 79:1610–1620; Garcia-Moreno E. et al., 1997, Biophys. Chem. 64:2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ee4073bc40a702b1f4bb7ba1263743
https://doi.org/10.1016/s0006-3495(02)75670-1
https://doi.org/10.1016/s0006-3495(02)75670-1
Autor:
Yung-Hsiang Kao, E Bertrand García-Moreno, Juliette T. J. Lecomte, Carolyn A. Fitch, Christopher J. Sarkisian, Shibani Bhattacharya
Publikováno v:
Biophysical Journal. 79(3):1637-1654
The salt dependence of histidine pK(a) values in sperm whale and horse myoglobin and in histidine-containing peptides was measured by (1)H-NMR spectroscopy. Structure-based pK(a) calculations were performed with continuum methods to test their abilit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d508e4147f24cbf6c74fc47c0600f92
Publikováno v:
Biophysical Journal. 100(3)
Internal ionizable groups are essential for energy transduction processes. They usually titrate with highly perturbed pKa values; the molecular determinants of these pKa values are poorly understood. Structure-based calculation of the pKa values of i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cabc5f0cd87479c0794ba515d30946c3
Autor:
Jamie L. Schlessman, Maja Cieplak, B.M. Doctrow, Ananya Majumdar, Carlos A. Castañeda, Bertrand Garcia-Moreno, Carolyn A. Fitch
Publikováno v:
Biophysical Journal. 100(3)
The active site of staphylococcal nuclease (SNase) has a cluster of four carboxylic residues, two with near normal pKa values, one (Asp-19) with a low pKa of 2.1, and one (Asp-21) with an unusually elevated pKa of 6.5. Crystal structures provide litt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4c7c24aad9005e4794f99e1983cd661
Autor:
Carlos A, Castañeda, Carolyn A, Fitch, Ananya, Majumdar, Victor, Khangulov, Jamie L, Schlessman, Bertrand E, García-Moreno
Publikováno v:
Proteins. 77(3)
Prior computational studies of the acid-unfolding behavior of staphylococcal nuclease (SNase) suggest that the pK(a) values of its carboxylic groups are difficult to reproduce with electrostatics calculations with continuum methods. To examine the mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ad62f20d39fc1d36c2e20a48162727a5
https://pubmed.ncbi.nlm.nih.gov/19533744
https://pubmed.ncbi.nlm.nih.gov/19533744