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protein secondary structure estimation program software sse 338  (JASCO Inc)


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    Structured Review

    JASCO Inc protein secondary structure estimation program software sse 338
    Protein Secondary Structure Estimation Program Software Sse 338, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+software+program/pm24913513-65-7-14
    Average 86 stars, based on 1 article reviews
    protein secondary structure estimation program software sse 338 - by Bioz Stars, 2026-09
    86/100 stars

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    Article Title: Zinc-L-carnosine binds to molecular chaperone HSP70 and inhibits the chaperone activity of the protein.
    Article Snippet: In this study, we have investigated the specific binding proteins of Zinc-L-carnosine (Polaprezinc) using Polaprezinc-affinity column chromatography in vitro.. A protein having a 70-kDa molecular mass was eluted by the linear gradient of 0 1.0mM Polaprezinc from the affinity column and the protein was identified as the molecular chaperone HSP70 by immunoblotting.. The chaperone activity of HSP70 was completely suppressed by Polaprezinc.

    Software:

    Article Title: Digestibility and structural properties of thermal and high hydrostatic pressure treated sweet potato (Ipomoea batatas L.) protein.
    Article Snippet: This study assessed the effects of thermal (40, 60, 80, 100 and 127 °C) and high hydrostatic pressure (HHP, 200, 400 and 600 MPa) treatments on the in vitro digestibility and structural properties of sweet potato protein (SPP).. The results showed that the in vitro digestibility of SPP increased significantly with increasing heating temperature and heating time (0–60 min), while HHP treatment had little or no effect.. Native SPP denaturation temperature (Td) and enthalpy change (ΔH) were 89.0 °C and 9.6 J/g, respectively.

    Article Title: Refolding, isolation and characterization of crystallizable human interferon-alpha 8 expression in Saccharomyces cerevisiae.
    Article Snippet: Human interferon-a8 was expressed in Saccharomyces crrevisiae and found to accumulate intracellularly in an insoluble form.. The protein could be solubilized and converted to a biologically active form with high yield by a denaturation-refolding procedure.. The interferon-as was further purified to apparent homogeneity by copper-chelate affinity chromatography and anion-cxchangc chromatography and fully characterized by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE), N-terminal sequence analysis, mass spectrometry, circular-dichroism (CD) spectroscopy and specific activity.

    Circular Dichroism:

    Article Title: Refolding, isolation and characterization of crystallizable human interferon-alpha 8 expression in Saccharomyces cerevisiae.
    Article Snippet: Human interferon-a8 was expressed in Saccharomyces crrevisiae and found to accumulate intracellularly in an insoluble form.. The protein could be solubilized and converted to a biologically active form with high yield by a denaturation-refolding procedure.. The interferon-as was further purified to apparent homogeneity by copper-chelate affinity chromatography and anion-cxchangc chromatography and fully characterized by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE), N-terminal sequence analysis, mass spectrometry, circular-dichroism (CD) spectroscopy and specific activity.



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