Pub. Date : 2015 Feb 12
PMID : 25672880
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Our results suggest that the serine plays a crucial role in maintaining the closed conformation of wild-type GK and the GMP recognition. | guanosine 5'-monophosphorothioate | guanylate kinase 1 | Homo sapiens |
| 2 | Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant. | guanosine 5'-monophosphorothioate | guanylate kinase 1 | Homo sapiens |
| 3 | Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant. | guanosine 5'-monophosphorothioate | guanylate kinase 1 | Homo sapiens |
| 4 | Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant. | guanosine 5'-monophosphorothioate | guanylate kinase 1 | Homo sapiens |
| 5 | Furthermore, the free energy profiles (FEPs) obtained by metadymanics clearly demonstrate that the open-closed conformational transition in WT GK is positive correlated with the process of GMP binding, indicating the GMP-induced closing motion of GK enzyme, which is not observed in the mutant. | guanosine 5'-monophosphorothioate | guanylate kinase 1 | Homo sapiens |