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  • 1
    Electronic Resource
    Electronic Resource
    Rattlesnake presynaptic neurotoxins: primary structure and evolutionary origin of the acidic subunit (1985)
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 7054-7058 
    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/bi00346a005
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Spider silk: the unraveling of a mystery (1992)
    s.l. : American Chemical Society
    Accounts of chemical research 25 (1992), S. 392-398 
    Details
    ISSN: 1520-4898
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ar00021a002
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Photoactivated heterobifunctional cross-linking reagents which demonstrate the aggregation state of phospholipase A2 (1977)
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 5650-5654 
    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/bi00644a041
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Photoactivated heterobifunctional cross-linking reagents which demonstrate the aggregation state of phospholipase A2 (1977)
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 5650-5654 
    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/bi00644a042
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of hypnosis on plasma proenkephalin peptide F and perceptual and cardiovascular responses during submaximal exercise (1992)
    Springer
    European journal of applied physiology 65 (1992), S. 573-578 
    Details
    ISSN: 1439-6327
    Keywords: Enkephalins ; Endogenous opioid peptides ; Endurance exercise
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Little information is available concerning the influence of subconscious mechanisms on neuroendocrine function, more specifically, proenkephalin peptide F release. Ten men [5 middle distance runners (21.6 (SD 0.54 years) and 5 untrained men (24.0 (SD 4.3 years)] consented to be volunteers in this investigation. Submaximal exercise intensities of 25% and 50& of peak oxygen consumption ({ie573-1}) (8 min stages) were used for both the control and hypnosis treatments. A traditional hypnotic induction was used, with the suggestion of two higher intensities of exercise stress (50% and 75% peak {ie573-2}) previously experienced in familiarization and testing by each subject. Each minute oxygen consumption was measured using open circuit spirometry, heart rate via an ECG, and ratings of perceived exertion (RPE) using the Borg scale. Plasma peptide F immunoreactivity (ir) [preproenkephalin-(107–140)] in blood sampled from an indwelling cannula was measured by radioimmunoassay at 7–8 min of each stage of the exercise test. Expected significant increases were observed for all cardiorespiratory and perceptual variables over the increasing exercise intensities and there were no significant differences between trained and untrained groups for peptide F it response patterns. Hypnosis did not significantly affect peptide F it concentrations (P 〉 0.05) and did not significantly alter exercise heart rate, RPE or minute ventilation (P 〉 0.05). However, hypnosis did significantly increase oxygen consumption during exercise (P = 0.0095) but not of the magnitude needed for the metabolic demands of the higher exercise intensities. Thus, traditional hypnosis was unable to make functionally significant changes in the cardiorespiratory variables. Training did not alter responses to exercise under hypnosis. The results of this study indicate that when using traditional hypnosis and a suggestion of harder exercise in highly selected groups, it may not be possible functionally to stress adrenal medullary secretion of proenkephalin fragments, RPE or cardiorespiratory variables.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00602368
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  • 6
    Electronic Resource
    Electronic Resource
    Secondary structure characteristics of proenkephalin peptides E, B, and F (1990)
    Springer
    Neurochemical research 15 (1990), S. 393-399 
    Details
    ISSN: 1573-6903
    Keywords: Opioid peptide ; enkephalin containing polypeptide ; conformation ; structure-function relationships
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The conformations of three adrenal medullary enkephalin containing polypeptides (ECPs) were investigated to gain an understanding of their potential structure-activity relationships. Secondary structure characteristics of peptides E, B, and F were examined by circular dichrosim (CD) under conditions designed to mimic both the soluble state and the anisotropic environment which exists at the biological effector site. Conformational differences between the three peptides were further examined by Fourier Transform Infrared Spectroscopy (FTIR) and by empirical predictions for conformation and hydrophobic periodicity. Although all three peptides have a similar structure, existing in random confirgurations in aqueous solutions, they do exhibit unique individual potentials to assume secondary structure in less polar environments. These conformational differences may be important factors in determining their unique individual biological activities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00969924
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    The effects of surface adsorption on the thermal stability of proteins (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 8-15 
    Details
    ISSN: 0006-3592
    Keywords: adsorption ; silica ; proteins ; lysozyme ; surface polarity ; protein stability ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of surface adsorption on the structure and stability of proteins is a matter of increasing interest in biotechnology. Therefore, we have examined the effect of adsorption to silica on the thermal stability of 7 proteins employing differential scanning calorimetry (DSC) and front surface fluorescence (FSF) spectroscopy. In general, it was found that surface adsorption decreased the thermal stability of the bound protein. Using lysozyme for further studies, DSC, FSF, and FTIR spectroscopies, as well as enzymatic activity measurements, were used to explore the effect of decreasing surface apolarity on stability. It was observed that increasing surface apolarity produced decreasing stability and increasing structural alteration of the adsorbed protein.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260400103
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    Structural studies of spider silk proteins in the fiber (1997)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 10 (1997), S. 1-6 
    Details
    ISSN: 0952-3499
    Keywords: dragline silk ; major ampullate ; protein structure ; NMR X-ray diffraction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Although spider silk has been studied for a number of years the structures of the proteins involved have yet to be definitely determined. X-ray diffraction and solid-state nuclear magnetic resonance (NMR) were used to study major ampullate (dragline) silk from Nephila clavipes. The silk was studied in its natural state, in the supercontacted state and in the restretched state following supercontraction. The natural silk structure is dominated by β-sheets aligned parallel to the fiber axis. Supercontraction is characterized by randomizing of the orientation of the β-sheet. When the fiber is restretched alignment is regained. However, the same reorientation was observed for wetting of minor ampullate silk which does not supercontract. Thus, the reorientation of β-sheets alone cannot explain the supercontraction in dragline silk. Cocoon silk showed very little β-sheet orientation in the natural state and there were no changes upon wetting. NMR and X-ray diffraction data are consistent with the β-sheets arising from the poly-alanine sequences known to be present in the proteins of major ampullate silk as has been proposed previously. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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