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origin 2018 version 8.1) software  (OriginLab corp)


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    OriginLab corp origin 2018 version 8.1) software
    Origin 2018 Version 8.1) Software, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/moe+software+version+2018/origin+2018+version+8+1++software/ppr0803371-69-0-2
    Average 90 stars, based on 1 article reviews
    origin 2018 version 8.1) software - by Bioz Stars, 2026-10
    90/100 stars

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    Software:

    Article Title: Fmoc-FF hydrogels and nanogels for improved and selective delivery of Dexamethasone in leukemic cells and diagnostic applications
    Article Snippet: .. Origin 2018 (OriginLab Corporation, version 8.1) software was used to arrange the comparative CD analysis. .. 2.7 Fourier Transform Infrared spectroscopy (FT-IR) FT-IR spectra of lled and nude Fmoc-FF nanogels were captured using a Jasco FT/IR 4100 spectrometer (Easton, MD) in an attenuated total re ection (ATR) mode and using a Ge single-crystal at a resolution of 4 cm− 1.

    Article Title: Fmoc-FF hydrogels and nanogels for improved and selective delivery of dexamethasone in leukemic cells and diagnostic applications
    Article Snippet: .. Origin 2018 (OriginLab Corporation, version 8.1) software was used to arrange the comparative CD analysis. .. FT-IR spectra of filled and empty HGs and NGs were captured using a Jasco FT/IR 4100 spectrometer (Easton, MD) in an attenuated total reflection (ATR) mode and using a Ge single-crystal at a resolution of 4 cm −1 .



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    Interface contact residues in the GPcl–NPC1complexes. ( A ) Residue contact pairs of the GPcl–NPC1 interfaces <t>for</t> <t>EBOV,</t> SUDV, and RAVV were analyzed using the <t>MOE</t> software (version 2018; Chemical Computing Group, Montreal, Canada). Residue–residue contact pairs that appeared in at least 50% of the 1500 MD simulation frames are shown for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes. In each panel, the light, intermediate dark, and darkest colors represent the contact pairs containing van der Waals interactions (vdW), vdW + hydrogen bonds (hb), and vdW + hb + salt bridges (sb), respectively. Amino acid residues that are distinct from those of EBOV GPcl are shown in red. The numbering scheme for GPcl was adapted from EBOV. ( B ) Venn diagram for the number of residue contact pairs observed for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes.
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    Interface contact residues in the GPcl–NPC1complexes. ( A ) Residue contact pairs of the GPcl–NPC1 interfaces for EBOV, SUDV, and RAVV were analyzed using the MOE software (version 2018; Chemical Computing Group, Montreal, Canada). Residue–residue contact pairs that appeared in at least 50% of the 1500 MD simulation frames are shown for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes. In each panel, the light, intermediate dark, and darkest colors represent the contact pairs containing van der Waals interactions (vdW), vdW + hydrogen bonds (hb), and vdW + hb + salt bridges (sb), respectively. Amino acid residues that are distinct from those of EBOV GPcl are shown in red. The numbering scheme for GPcl was adapted from EBOV. ( B ) Venn diagram for the number of residue contact pairs observed for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes.

    Journal: Viruses

    Article Title: Structural Insights into the Interaction of Filovirus Glycoproteins with the Endosomal Receptor Niemann-Pick C1: A Computational Study

    doi: 10.3390/v13050913

    Figure Lengend Snippet: Interface contact residues in the GPcl–NPC1complexes. ( A ) Residue contact pairs of the GPcl–NPC1 interfaces for EBOV, SUDV, and RAVV were analyzed using the MOE software (version 2018; Chemical Computing Group, Montreal, Canada). Residue–residue contact pairs that appeared in at least 50% of the 1500 MD simulation frames are shown for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes. In each panel, the light, intermediate dark, and darkest colors represent the contact pairs containing van der Waals interactions (vdW), vdW + hydrogen bonds (hb), and vdW + hb + salt bridges (sb), respectively. Amino acid residues that are distinct from those of EBOV GPcl are shown in red. The numbering scheme for GPcl was adapted from EBOV. ( B ) Venn diagram for the number of residue contact pairs observed for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes.

    Article Snippet: Residue–residue contacts between NPC1-C and GPcl from EBOV, SUDV, and RAVV were analyzed using the Protein Contacts in Molecular Operating Environment (MOE) software (version 2018; Chemical Computing Group, Montreal, QC, Canada).

    Techniques: Software

    Differences in the GPcl–NPC1 binding structures between EBOV, SUDV, and RAVV. ( A ) Residue contact pairs of the GPcl–NPC1 interfaces for EBOV, SUDV, and RAVV were analyzed using the MOE software (version 2018; Chemical Computing Group, Montreal, Canada). Residue–residue contact pairs that appeared in at least 50% of the 1500 MD simulation frames, are shown for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes. In each panel, the light, intermediate dark, and darkest colors represent the contact pairs containing van der Waals interactions (vdW), vdW + hydrogen bonds (hb), and vdW + hb + salt bridges (sb), respectively. Amino acid residues that are distinct from those of EBOV GPcl are shown in red. The numbering scheme for GPcl was adapted from EBOV. ( B ) Venn diagram for the number of residue contact pairs observed for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes.

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    Article Title: Structural Insights into the Interaction of Filovirus Glycoproteins with the Endosomal Receptor Niemann-Pick C1: A Computational Study

    doi: 10.3390/v13050913

    Figure Lengend Snippet: Differences in the GPcl–NPC1 binding structures between EBOV, SUDV, and RAVV. ( A ) Residue contact pairs of the GPcl–NPC1 interfaces for EBOV, SUDV, and RAVV were analyzed using the MOE software (version 2018; Chemical Computing Group, Montreal, Canada). Residue–residue contact pairs that appeared in at least 50% of the 1500 MD simulation frames, are shown for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes. In each panel, the light, intermediate dark, and darkest colors represent the contact pairs containing van der Waals interactions (vdW), vdW + hydrogen bonds (hb), and vdW + hb + salt bridges (sb), respectively. Amino acid residues that are distinct from those of EBOV GPcl are shown in red. The numbering scheme for GPcl was adapted from EBOV. ( B ) Venn diagram for the number of residue contact pairs observed for EBOV (blue), SUDV (red), and RAVV (yellow) GPcl–NPC1 complexes.

    Article Snippet: Residue–residue contacts between NPC1-C and GPcl from EBOV, SUDV, and RAVV were analyzed using the Protein Contacts in Molecular Operating Environment (MOE) software (version 2018; Chemical Computing Group, Montreal, QC, Canada).

    Techniques: Binding Assay, Software