Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Melinda M. Dixon"'
Autor:
Katherine A. Pattridge, Melinda M. Dixon, Martha L. Ludwig, Anita L. Metzger, Mesut Eren, Richard P. Swenson, Yucheng Feng
Publikováno v:
Biochemistry. 36:1259-1280
X-ray analyses of wild-type and mutant flavodoxins from Clostridium beijerinckii show that the conformation of the peptide Gly57-Asp58, in a bend near the isoalloxazine ring of FMN, is correlated with the oxidation state of the FMN prosthetic group.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c75448ffba521a98242ed8bb5d1c53
https://doi.org/10.1021/bi962180o
https://doi.org/10.1021/bi962180o
Publikováno v:
Structure. 4:1263-1275
Background In both mammalian and microbial species, B 12 -dependent methionine synthase catalyzes methyl transfer from methyltetrahydrofolate (CH 3 –H 4 folate) to homocysteine. The B 12 (cobalamin) cofactor plays an essential role in this reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feaf44d1965830599a889424247f9c51
https://doi.org/10.1016/s0969-2126(96)00135-9
https://doi.org/10.1016/s0969-2126(96)00135-9
Publikováno v:
International Journal of Biological Macromolecules. 13:89-96
Crystals of gamma-chymotrypsin (gamma-CHT) grown at pH 7.0 are stable from pH 2.0 to 11.0. Crystalline gamma-CHT therefore provides an unusually favourable system to observe the structure of a protein and its bound solvent over a broad range of pH. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::264a832248e5ebb68ec2cdee18e96e2c
https://doi.org/10.1016/0141-8130(91)90054-x
https://doi.org/10.1016/0141-8130(91)90054-x
Autor:
Martha L. Ludwig, Catherine L. Drennan, David M. Hoover, Rowena G. Matthews, Melinda M. Dixon, Joseph T. Jarrett, Celia W. Goulding
Publikováno v:
Vitamin B12 and B12-Proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de52935f35500698c9572e12b9a790e5
https://doi.org/10.1002/9783527612192.ch07
https://doi.org/10.1002/9783527612192.ch07
Publikováno v:
S-Adenosylmethionine-Dependent Methyltransferases: Structures And Functions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09e2c42fe1a32f04f04b693d50b97e1c
https://doi.org/10.1142/9789812813077_0002
https://doi.org/10.1142/9789812813077_0002
Publikováno v:
Nature. 375(6526)
The structural end-points of haemoglobin's transition from its low-oxygen-affinity (T) to high-oxygen-affinity (R) state, have been well established by X-ray crystallography, but short-lived intermediates have proved less amenable to X-ray studies. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc51ec2e7964623c1fef0f2230c1c13c
https://pubmed.ncbi.nlm.nih.gov/7723849
https://pubmed.ncbi.nlm.nih.gov/7723849
Autor:
Myoung Soo Lah, Katherine A. Pattridge, James A. Fee, Melinda M. Dixon, Martha L. Ludwig, William C. Stallings
Publikováno v:
Biochemistry. 34(5)
The crystal structure of dimeric Fe(II1) superoxide dismutase (SOD) from Escherichia coli (3006 protein atoms, 2 irons, and 28 1 solvents) has been refined to an R of 0.184 using all observed data between 40.0 and 1.85 8, (34 879 reflections). Featur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1da77952c081af2f791a4bcf6ac48760
https://pubmed.ncbi.nlm.nih.gov/7849024
https://pubmed.ncbi.nlm.nih.gov/7849024
Autor:
Melinda M. Dixon, Brian W. Matthews
Publikováno v:
Biochemistry. 28:7033-7038
Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) J. Mol. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab1c3133b35e10931c04bfac24b76f64
https://doi.org/10.1021/bi00443a038
https://doi.org/10.1021/bi00443a038