Add to ORKGTriosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconversion of dihydroxyacetonephosphate and D-glyceraldehyde-3-phosphate. The reaction catalysed by TIM has been highly characterised at the biochemical level, and therefore the enzyme is an ideal target for structural analysis in order to achieve understanding of the structure function relationship. ... Zie: Summar
This thesis discusses the structure-function studies on triosephosphate isomerase (TIM) from Plasmod...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Crystallographic binding studies have been carried out to probe the active-site binding properties o...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Abstract The triosephosphate isomerase (TIM) barrel superfamily is a broad family of proteins, most ...
Abstract The aim of this PhD-study was to better understand the structure-function relationship of ...
AbstractTIM catalyses the interconversion of a triosephosphate aldehyde into a triosephosphate keton...
This thesis describes studies directed towards understanding structure-function relationships of tri...
AbstractTriosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active s...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
This thesis discusses the structure-function studies on triosephosphate isomerase (TIM) from Plasmod...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Crystallographic binding studies have been carried out to probe the active-site binding properties o...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Triosephosphate isomerase (TIM) is an enzyme of the glycolytic pathway which catalyses the interconv...
Abstract The triosephosphate isomerase (TIM) barrel superfamily is a broad family of proteins, most ...
Abstract The aim of this PhD-study was to better understand the structure-function relationship of ...
AbstractTIM catalyses the interconversion of a triosephosphate aldehyde into a triosephosphate keton...
This thesis describes studies directed towards understanding structure-function relationships of tri...
AbstractTriosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active s...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
This thesis discusses the structure-function studies on triosephosphate isomerase (TIM) from Plasmod...
Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis i...
Crystallographic binding studies have been carried out to probe the active-site binding properties o...