Thermostability of proteins from Thermotoga maritima.
Jaenicke
R
R
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Regensburg D-93040, Germany.
Böhm
G
G
D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000378:metabolism; D004795:Enzyme Stability; D005969:Glutamate Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000378:metabolism; D006358:Hot Temperature; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D010735:Phosphoglycerate Kinase / Q000737:chemistry / Q000378:metabolism; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D020124:Thermotoga maritima / Q000201:enzymology*; D014305:Triose-Phosphate Isomerase / Q000737:chemistry / Q000378:metabolism
D011506:Proteins; D011994:Recombinant Proteins; D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005969:Glutamate Dehydrogenase; D013762:Tetrahydrofolate Dehydrogenase; D010735:Phosphoglycerate Kinase; D010751:Phosphopyruvate Hydratase; D019747:Aldose-Ketose Isomerases; D014305:Triose-Phosphate Isomerase; C029865:phosphoribosylanthranilate isomerase