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Günter Maass

Researcher at Hochschule Hannover

Publications -  34
Citations -  1464

Günter Maass is an academic researcher from Hochschule Hannover. The author has contributed to research in topics: EcoRI & Restriction enzyme. The author has an hindex of 25, co-authored 34 publications receiving 1453 citations.

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Linear diffusion of restriction endonucleases on DNA.

TL;DR: It is concluded that linear diffusion, albeit detectable under certain conditions in vitro, probably is of little importance for the process of site localization in vivo.
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Cystic fibrosis with three mutations in the cystic fibrosis transmembrane conductance regulator gene.

TL;DR: Three mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene were discovered in a pancreas-insufficient patient with CF who displayed an uncommon combination of almost normal chloride concentration in sweat tests and typical symptoms of gastrointestinal and pulmonary disease.
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Substrate-assisted catalysis in the cleavage of DNA by the EcoRI and EcoRV restriction enzymes

TL;DR: Experimental evidence is presented to support the proposed idea that the attacking water molecule is activated by the negatively charged pro-Rp phosphoryl oxygen of the phosphate group 3' to the scissile phosphodiester bond and gives a straightforward explanation of why in the EcoRI-DNA and EcoRV-DNA complexes the DNA is distorted differently, but in each case the 3' phosphate group closely approaches the phosphategroup that is attacked.
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Changing the hydrogen-bonding potential in the DNA binding site of EcoRI by site-directed mutagenesis drastically reduces the enzymatic activity, not, however, the preference of this restriction endonuclease for cleavage within the site-GAATTC-.

TL;DR: A detailed analysis of the steady-state kinetics of cleavage of pUC8 DNA and a tridecadeoxynucleotide substrate demonstrates that the reduction in activity for all DNA binding site mutants investigated so far is mainly due to a decrease in kcat, with the exception of the Arg200 to Lys mutant, which is only impaired in its KM.
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The conformational transitions in yeast tRNAPhe as studied with tRNAPhe fragments.

TL;DR: The thermal denaturation process of intact tRNAPhe can be interpreted as follows: at first the tertiary structure is converted to a cloverleaf-like structure; this process is followed by the melting of the acceptor and anticodon stems; finally the ribosylthymine and dihydrouridine stems dissociate independently.