Chaperonins and protein folding.
Baneyx
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Department of Chemical Engineering, University of Washington, Seattle 98195.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D018835:Chaperonin 10 / Q000235:genetics / Q000502:physiology; D018834:Chaperonin 60 / Q000235:genetics / Q000502:physiology; D018833:Chaperonins / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D000255:Adenosine Triphosphate; D013762:Tetrahydrofolate Dehydrogenase; D000251:Adenosine Triphosphatases; D018833:Chaperonins; C063842:dnaK protein, E coli