Hans-Werner Adolph

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MOTIVATION Functional annotation of unknown proteins is a major goal in proteomics. A key annotation is the prediction of a protein's subcellular localization. Numerous prediction techniques have been developed, typically focusing on a single underlying biological aspect or predicting a subset of all possible localizations. An important step is taken(More)
Functional annotation of unknown proteins is a major goal in proteomics. A key step in this annotation process is the definition of a protein's subcellular lo-calization. As a consequence, numerous prediction techniques for localization have been developed over the years. These methods typically focus on a single underlying biological aspect or predict a(More)
The use of substrate analogues as inhibitors provides a way to understand and manipulate enzyme function. Here we report two 1 A resolution crystal structures of liver alcohol dehydrogenase in complex with NADH and two inhibitors: dimethyl sulfoxide and isobutyramide. Both structures present a dynamic state of inhibition. In the dimethyl sulfoxide complex(More)
Motivation: Functional annotation of unknown proteins is a major goal in proteomics. A key annotation is the prediction of a protein's subcellular localization. Numerous prediction techniques have been developed, typically focusing on a single underlying biological aspect or predicting a subset of all possible localizations. An important step is taken(More)
Functional annotation of unknown proteins is amajor goal in proteomics. Ak ey step in this annotation process is thed efinition of ap rotein'ss ubcellular lo-calization. As ac onsequence, numerous predictiont echniques for localization have been developed overthe years. These methods typically focus on asingle underlying biological aspect or predict asubset(More)
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