Zobrazeno 1 - 10
of 50
pro vyhledávání: '"G K Ackers"'
Publikováno v:
Proteins.
The contribution of the alpha(1)beta(1)half-oxygenated tetramer [alphabeta:alphaO(2)betaO(2)] (species 21) to human hemoglobin cooperativity was evaluated using cryogenic isoelectric focusing. The cooperative free energy of binding, reflecting O(2)-d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::39aa6482741ba077770f5110afab5b07
https://pubmed.ncbi.nlm.nih.gov/11013398
https://pubmed.ncbi.nlm.nih.gov/11013398
Publikováno v:
Methods in enzymology. 295
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ea87d1723f19992d61586073d04f4f67
https://pubmed.ncbi.nlm.nih.gov/9750232
https://pubmed.ncbi.nlm.nih.gov/9750232
Autor:
A L, Klinger, G K, Ackers
Publikováno v:
Methods in enzymology. 295
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::34cf1e81e0b6fb974f0cc743d4f5f3f3
https://pubmed.ncbi.nlm.nih.gov/9750220
https://pubmed.ncbi.nlm.nih.gov/9750220
Autor:
G K, Ackers
Publikováno v:
Advances in protein chemistry. 51
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::19b699cefba3d24946c274e082abc33c
https://pubmed.ncbi.nlm.nih.gov/9615171
https://pubmed.ncbi.nlm.nih.gov/9615171
Publikováno v:
Methods in enzymology. 232
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d3f105dbbe53424a22ccdcfa4bbfecdb
https://pubmed.ncbi.nlm.nih.gov/8057881
https://pubmed.ncbi.nlm.nih.gov/8057881
Publikováno v:
Methods in enzymology. 210
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2606ba84c254867a31f27bf852e7c37c
https://pubmed.ncbi.nlm.nih.gov/1584044
https://pubmed.ncbi.nlm.nih.gov/1584044
Autor:
K S, Koblan, G K, Ackers
Publikováno v:
Biochemistry. 30(31)
The effects of monovalent salt activity on the site-specific and cooperative interactions of cI repressor with its three operator sites OR were studied by using quantitative DNase I footprint titration methods. Individual-site binding isotherms were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1749ed4618ab07babaace5a7985fa4fe
https://pubmed.ncbi.nlm.nih.gov/1831046
https://pubmed.ncbi.nlm.nih.gov/1831046
Publikováno v:
Biochemistry. 30(29)
Cooperative free energies have been determined for the 10 ligation species of human hemoglobin in the Co(II)/Fe(II)-CO system. In this system, subunits containing unligated cobaltous hemes coexist in the same tetramer with naturally occurring ferrous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::283f7cd416dd6446380a03e891889035
https://pubmed.ncbi.nlm.nih.gov/1854735
https://pubmed.ncbi.nlm.nih.gov/1854735
Publikováno v:
Biophysical chemistry. 35(1)
Reaction of tetrameric hemoglobin with ligands at the four heme sites yields nine species that have structurally unique combinations of ligated and unligated subunits. Using hemoglobins where the ligated subunits contain cyanomethemoglobin, Smith and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0bb8d59aa720b5ab6c9fd5c79afdb6a2
https://pubmed.ncbi.nlm.nih.gov/2328279
https://pubmed.ncbi.nlm.nih.gov/2328279
Autor:
R Valdes, G K Ackers
Publikováno v:
Journal of Biological Chemistry. 252:88-91
Calorimetric heats generated upon mixing solutions of alphaSH and betaSH chains of human hemoglobin have been studied by isothermal heatburst microcalorimetry as a function of mixture composition. Based upon studies described in accompanying papers,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f701a7a976d34edf207a45b28835de49
https://doi.org/10.1016/s0021-9258(17)32802-8
https://doi.org/10.1016/s0021-9258(17)32802-8