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  • 1
    Electronic Resource
    Electronic Resource
    5-Hydroxytryptophan: An absorption and fluorescence probe which is a conservative replacement for [A14 tyrosine] in insulin (1995)
    Springer
    The protein journal 14 (1995), S. 225-232 
    Details
    ISSN: 1573-4943
    Keywords: 5-Hydroxytryptophan ; tryptophan ; insulin analogs ; fluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Use of insulin's intrinsic tyrosine absorption and fluorescence to monitor its interaction with the insulin receptor is limited because the spectral properties of the receptor tryptophan residues mask the spectral properties of the hormone tyrosine residues. We describe the synthesis of an insulin analog where A14 tyrosine is replaced by a tryptophan analog, 5-hydroxytryptophan. This insulin is spectrally enhanced since 5-hydroxytryptophan has an absorption band above 300 nm which is at lower energies than the absorption of tryptophan. Steady-state and time-resolved fluorescence parameters indicate that 5-hydroxytryptophan reports the same information about the environment of the A14 side chain as does the corresponding tryptophan-containing insulin. The synthetic hormone is a full agonist compared to porcine insulin, but has slightly reduced specific activity. Consequently, this spectrally enhanced insulin analog will be useful for hormone-receptor interaction studies since it can be observed by both absorption and fluorescence even in the presence of the tryptophan-containing receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886763
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Effects on protein structure and function of replacing tryptophan with 5-hydroxytryptophan: Single-tryptophan mutants of the N-terminal domain of the bacteriophage λ repressor (1996)
    Springer
    The protein journal 15 (1996), S. 77-86 
    Details
    ISSN: 1573-4943
    Keywords: 5-Hydroxytryptophan ; tryptophan ; conformational energy computations ; λ-repressor mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Conformational energy computations have been carried out on the N-acetyl-N′-methylamide of 5-hydroxytryptophan (5OH-Trp) using ECEPP/3. As observed with tryptophan (Trp), the most preferred conformation about theC α −C β bond of the side chain isg + ort. This preference is reduced to only thet conformational state when 5-hydroxyTrp is in the middle of a right-handed poly(l-alanine)α-helix. A similar result has been obtained with Trp [Pielaet al. (1987),Biopolymers 1987, 1273–1286]. These results suggest that replacement of Trp by its analog 5-hydroxyTrp may be tolerated in anα-helix. To test this hypothesis, we have replaced Trp by 5OH-Trp in the fifth helices of two functionally active mutants of the N-terminal domain of the bacteriophage λ repressor. Computations on the packing of these helices have shown that no significant structural changes result from the replacement of Trp by 5OH-Trp. The DNA-binding activity of these mutants, as assessed indirectly through geometrical parameters, is also unaltered.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886813
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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