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  • 1
    Electronic Resource
    Electronic Resource
    Selective removal of a Si0.7Ge0.3 layer from Si(100) (1991)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 58 (1991), S. 1899-1901 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The selective removal of epitaxial Si0.7Ge0.3 from {100} silicon using an aqueous based etch is reported. An etch consisting of HNO3:H2O:HF(0.5%), 40:20:5 at 22 °C, removes Si0.7Ge0.3 at a rate of 207 A(ring)/min, and removes {100} Si at a rate of 16 A(ring)/min. This corresponds to a selectivity of 1321 where the selectivity is defined as the ratio of the Si0.7Ge0.3 to {100} Si etch rates. This etch leaves the surface smooth and free from pitting or trenching as observed by optical microscopy. The results obtained are consistent with a germanium enhanced oxidation mechanism of the Si0.7Ge0.3 alloy during semiconductor removal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.105067
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of amino acid residues photolabeled with 8-azidoadenosine 5'-diphosphate in the catalytic site of sarcoplasmic reticulum calcium-ATPase (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 3414-3421 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00064a027
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  • 3
    Electronic Resource
    Electronic Resource
    Stochastic modeling of fast kinetics in a radiation track (1990)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 94 (1990), S. 251-258 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100364a041
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  • 4
    Electronic Resource
    Electronic Resource
    A reply (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Anaesthesia 46 (1991), S. 0 
    Details
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2044.1991.tb11727.x
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  • 5
    Electronic Resource
    Electronic Resource
    Evolutionary Relationships within the Family of P-Type Cation Pumps (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 671 (1992), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1992.tb43788.x
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms (1993)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 49 (1993), S. 490-496 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Aldehyde reductase from porcine kidney has been crystallized from buffered ammonium sulfate solutions. Two crystal forms are monoclinic, space group P21, with a = 56.2, b = 98.1, c = 73.2 Å, β = 112.5° and a = 92.4, b = 62.1, c = 59.0 Å, β = 94.6°. A third crystal form is hexagonal with a = b = 166.0, c = 66.0 Å, α = β = 90.0° and γ = 120.0°. Molecular-replacement structure solutions have been successfully obtained for the two monoclinic crystal forms. The crystallographic R factor at 8–2.8 Å resolution for the two monoclinic crystal forms is currently 0.23 and 0.25, respectively. There are two molecules per asymmetric unit related by a non-crystallographic twofold axis. The aldehyde reductase models are supported by the arrangement of the molecules in their respective unit cells and by electron densities corresponding to amino-acid side chains not included in the search structures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993004044
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  • 7
    Electronic Resource
    Electronic Resource
    Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 859-868 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 Å resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 Å resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a β/α-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994005275
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  • 8
    Electronic Resource
    Electronic Resource
    Cross-channel traffic (1991)
    [s.l.] : Nature Publishing Group
    Nature 351 (1991), S. 450-451 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE introduction in the 1970s of single-channel conductance measurements on black lipid films and of patch clamping of membranes provided the ability to follow the opening and closing of single ion channels and to study the gating process. This led to advances in understanding which were well ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/351450b0
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  • 9
    Electronic Resource
    Electronic Resource
    The semiotics of charge (1991)
    [s.l.] : Nature Publishing Group
    Nature 351 (1991), S. 349-350 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] ON page 414 of this issue1, a group from Richard Klausner's laboratory describe results that will further constrain speculation about the function of charged residues in transmembfane segments. The paper, by Cosson et aL, is the latest of several that sub-stantiate the importance of such residues ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/351349a0
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  • 10
    Electronic Resource
    Electronic Resource
    A method for α-helical integral membrane protein fold prediction (1994)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 18 (1994), S. 281-294 
    Details
    ISSN: 0887-3585
    Keywords: membrane ; protein ; structure ; prediction ; G-protein coupled receptor ; rhodopsin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Integral membrane proteins (of the α-helical class) are of central importance in a wide variety of vital cellular functions. Despite considerable effort on methods to predict the location of the helices, little attention has been directed toward developing an automatic method to pack the helices together. In principle, the prediction of membrane proteins should be easier than the prediction of globular proteins: there is only one type of secondary structure and all helices pack with a common alignment across the membrane. This allows all possible structures to be represented on a simple lattice and exhaustively enumerated. Prediction success lies not in generating many possible folds but in recognizing which corresponds to the native. Our evaluation of each fold is based on how well the exposed surface predicted from a multiple sequence alignment fits its allocated position. Just as exposure to solvent in globular proteins can be predicted from sequence variation, so exposure to lipid can be recognized by variable-hydrophobic (variphobic) positions. Application to both bacteriorhodopsin and the eukaryotic rhodopsin/opsin families revealed that the angular size of the lipid-exposed faces must be predicted accurately to allow selection of the correct fold. With the inherent uncertainties in helix prediction and parameter choice, this accuracy could not be guaranteed but the correct fold was typically found in the top six candidates. Our method provides the first completely automatic method that can proceed from a scan of the protein sequence databanks to a predicted three-dimensional structure with no intervention required from the investigator. Within the limited domain of the seven helix bundle proteins, a good chance can be given of selecting the correct structure. However, the limited number of sequences available with a corresponding known structure makes further characterization of the method difficult. © 1994 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340180309
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