Zobrazeno 1 - 10
of 28
pro vyhledávání: '"W G, Hol"'
Publikováno v:
Journal of Biological Chemistry. 266:2953-2961
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6837a3c11dbdd2f18f92de583df4ef6f
https://doi.org/10.1016/s0021-9258(18)49940-1
https://doi.org/10.1016/s0021-9258(18)49940-1
Autor:
W G, Hol
Publikováno v:
Nature structural biology.
The field of robotics is affecting structural biology, enabling the era of structural genomics. The potential impact on protein fold prediction, biology, protein engineering and medicine is immense. Unraveling mysteries in the protein structure unive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d49b5cee436de6be35bc2798606ac29e
https://pubmed.ncbi.nlm.nih.gov/11104001
https://pubmed.ncbi.nlm.nih.gov/11104001
Publikováno v:
Journal of molecular biology. 302(5)
The enzyme 7,8-dihydropteroate synthase (DHPS) catalyzes the condensation of para-aminobenzoic acid (pABA) with 6-hydroxymethyl-7, 8-dihydropterin-pyrophosphate to form 7,8-dihydropteroate and pyrophosphate. DHPS is essential for the de novo synthesi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b2dda6309ebcfdb13c4ff2ae1db253d8
https://pubmed.ncbi.nlm.nih.gov/11007651
https://pubmed.ncbi.nlm.nih.gov/11007651
Publikováno v:
Proteins. 36(4)
A Monte Carlo procedure, encoded in the program Blob, has been developed and tested for the purpose of positioning large molecular fragments or small flexible molecules in electron density maps. The search performed by the algorithm appears to be suf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e00dd3f4a9a2ca19c4670d25ee2f86a5
https://pubmed.ncbi.nlm.nih.gov/10450093
https://pubmed.ncbi.nlm.nih.gov/10450093
Publikováno v:
Proteins. 36(4)
A significant portion of new protein structures contain folds that are related to those seen before. During the development of a computer program that can accurately position, in electron density maps, large protein domains with large structural devi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::485a8743ac73e1fdd6721e225384142d
https://pubmed.ncbi.nlm.nih.gov/10450094
https://pubmed.ncbi.nlm.nih.gov/10450094
Publikováno v:
Nature structural biology. 6(8)
The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::01d0319438bfb31126caca0d62403907
https://pubmed.ncbi.nlm.nih.gov/10426958
https://pubmed.ncbi.nlm.nih.gov/10426958
Publikováno v:
European journal of immunology. 28(4)
The Escherichia coli heat-labile enterotoxin (LT) is known for its potent mucosal immunoadjuvant activity towards co-administered antigens. LT is composed of one A subunit, which has ADP-ribosylation activity, and a homopentameric B subunit, which ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5c3b1c6539269e9d7f2834fbadf93ce1
https://pubmed.ncbi.nlm.nih.gov/9565364
https://pubmed.ncbi.nlm.nih.gov/9565364
Publikováno v:
Protein science : a publication of the Protein Society. 7(2)
Phosphoglycerate kinase (PGK) catalyzes the phosphoryl transfer between 1,3 bis-phosphoglycerate and ADP to form 3-phosphoglycerate and ATP, undergoing significant conformational changes during catalysis. To more precisely document this reaction and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4d0b815fe22479eb0d35fa8ed706a590
https://pubmed.ncbi.nlm.nih.gov/9521128
https://pubmed.ncbi.nlm.nih.gov/9521128
Publikováno v:
Protein science : a publication of the Protein Society. 6(4)
Members of the family of 2-oxoacid dehydrogenase multienzyme complexes catalyze the oxidative decarboxylation of alpha-keto acids and are among the most remarkable enzymatic machineries in the living cell. These multienzyme complexes combine a highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::47fd9e4d36617e22fa4d1fb7e5dae7fa
https://pubmed.ncbi.nlm.nih.gov/9098902
https://pubmed.ncbi.nlm.nih.gov/9098902
Publikováno v:
Protein science : a publication of the Protein Society. 3(5)
The crystal structure of recombinant human triosephosphate isomerase (hTIM) has been determined complexed with the transition-state analogue 2-phosphoglycolate at a resolution of 2.8 A. After refinement, the R-factor is 16.7% with good geometry. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::be678e8a99d21eec650791c4a85faff7
https://pubmed.ncbi.nlm.nih.gov/8061610
https://pubmed.ncbi.nlm.nih.gov/8061610