Search Results - "Aehle, W."

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  1. 1

    Zooming In on Metagenomics: Molecular Microdiversity of Subtilisin Carlsberg in Soil by Gabor, E., Niehaus, F., Aehle, W., Eck, J.

    Published in Journal of molecular biology (20-04-2012)
    “…Evolution has led to the development of a gigantic repertoire of microbial genes that can be exploited for industrial purposes. Due to microevolutionary…”
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  2. 2

    Construction of stabilized proteins by combinatorial consensus mutagenesis by Amin, N., Liu, A.D., Ramer, S., Aehle, W., Meijer, D., Metin, M., Wong, S., Gualfetti, P., Schellenberger, V.

    Published in Protein engineering, design and selection (01-11-2004)
    “…We constructed stabilized variants of β-lactamase (BLA) from Enterobacter cloacae by combinatorial recruitment of consensus mutations. By aligning the…”
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    Rational protein engineering and industrial application: structure prediction by homology and rational design of protein-variants with improved 'washing performance'--the alkaline protease from Bacillus alcalophilus by Aehle, W, Sobek, H, Amory, A, Vetter, R, Wilke, D, Schomburg, D

    Published in Journal of biotechnology (1993)
    “…The successful attempt is presented to engineer an enzyme with respect to its technical application by the use of computer-aided protein design techniques…”
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    X-ray structure determination and comparison of two crystal forms of a variant (Asn115Arg) of the alkaline protease from Bacillus alcalophilus refined at 1.85 A resolution by Sobek, H, Hecht, H J, Aehle, W, Schomburg, D

    Published in Journal of molecular biology (05-11-1992)
    “…The X-ray structure determination, refinement and comparison of two crystal forms of a variant (Asn115Arg) of the alkaline protease from Bacillus alcalophilus…”
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  7. 7

    Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4 Å resolution by SOBEK, H, HECHT, H. J, HOFMANN, B, AEHLE, W, SCHOMBURG, D

    Published in FEBS letters (12-11-1990)
    “…The crystal structure of an alkaline protease from Bacillus alcalophilus has been determined by X-ray diffraction at 2.4 A resolution. The enzyme crystallizes…”
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    Evaluation of protein 3-D structure prediction: Comparison of modelled and X-ray structure of an alkaline serine protease by Aehle, Wolfgang, Sobek, Harald, Schomburg, Dietmar

    Published in Journal of biotechnology (31-07-1995)
    “…We describe the modelling of the structure of the highly alkaline subtilisin protease OPTICLEAN from Bacillus alcalophilus. The model was developed through…”
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  13. 13

    Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4Åresolution by Sobek, H., Hecht, H.J., Hofmann, B., Aehle, W., Schomburg, D.

    Published in FEBS letters (12-11-1990)
    “…The crystal structure of an alkaline protease from Bacillus alcahphilus has been determined by X-ray diffraction at 2.4Åresolution. The enzyme crystallizes in…”
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  14. 14

    Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4 angstroms resolution by Sobek, H, Hecht, HJ, Hofmann, B, Aehle, W, Schomburg, D

    Published in FEBS letters (01-01-1990)
    “…The crystal structure of an alkaline protease from Bacillus alcalophilus has been determined by X-ray diffraction at 2.4 angstroms resolution. The enzyme…”
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  15. 15

    Structure/activity relationship of adenine‐modified NAD derivatives with respect to porcine heart lactate dehydrogenase isozyme H 4 simulated with molecular mechanics by HENDLE, Jörg, BÜCKMANN, Andreas F., AEHLE, Wolfgang, SCHOMBURG, Dietmar, SCHMID, Rolf D.

    Published in European journal of biochemistry (01-05-1993)
    “…Using a significantly simplifed modification procedure, four charged analogues of the coenzyme NAD, N (1)‐ and N 6 ‐(2‐hydroxy‐3‐trimethylammoniumpropyl)‐NAD,…”
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  16. 16

    Structure/activity relationship of adenine‐modified NAD derivatives with respect to porcine heart lactate dehydrogenase isozyme H4 simulated with molecular mechanics by HENDLE, Jörg, BÜCKMANN, Andreas F., AEHLE, Wolfgang, SCHOMBURG, Dietmar, SCHMID, Rolf D.

    Published in European journal of biochemistry (01-05-1993)
    “…Using a significantly simplifed modification procedure, four charged analogues of the coenzyme NAD, N(1)‐ and N6‐(2‐hydroxy‐3‐trimethylammoniumpropyl)‐NAD,…”
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    Journal Article