On the advantages of imperfect energetic linkage.
Leyh
T S
TS
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
D000250:Adenosine Phosphosulfate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D004250:DNA Topoisomerases, Type II / Q000378:metabolism; D004278:DNA, Superhelical / Q000737:chemistry; D004734:Energy Metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D007700:Kinetics; D008954:Models, Biological; D009154:Mutation; D010444:Peptide Elongation Factor Tu / Q000378:metabolism; D010724:Phosphoadenosine Phosphosulfate / Q000235:genetics / Q000494:pharmacology; D011487:Protein Conformation; D013430:Sulfate Adenylyltransferase / Q000378:metabolism
D004278:DNA, Superhelical; D010724:Phosphoadenosine Phosphosulfate; D000250:Adenosine Phosphosulfate; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D013430:Sulfate Adenylyltransferase; D010444:Peptide Elongation Factor Tu; D004250:DNA Topoisomerases, Type II