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af2000 tm af4 system  (Postnova Analytics)

 
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    Postnova Analytics af2000 tm af4 system
    Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique <t>(AF4).</t> (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.
    Af2000 Tm Af4 System, supplied by Postnova Analytics, 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/result/af2000 tm af4 system/product/Postnova Analytics
    Average 86 stars, based on 1 article reviews
    af2000 tm af4 system - by Bioz Stars, 2026-06
    86/100 stars

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    1) Product Images from "Thermo‐Chemically Modified Silk Scaffolds Reveal Niche‐Driven Regulation of Hematopoiesis and Fibrosis"

    Article Title: Thermo‐Chemically Modified Silk Scaffolds Reveal Niche‐Driven Regulation of Hematopoiesis and Fibrosis

    Journal: Small (Weinheim an Der Bergstrasse, Germany)

    doi: 10.1002/smll.202513071

    Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique (AF4). (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.
    Figure Legend Snippet: Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique (AF4). (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.

    Techniques Used: Dissolution, Molecular Weight, Field Flow Fractionation, Spectroscopy, Concentration Assay



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    Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique <t>(AF4).</t> (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.
    Af2000 Tm Af4 System, supplied by Postnova Analytics, 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/result/af2000 tm af4 system/product/Postnova Analytics
    Average 86 stars, based on 1 article reviews
    af2000 tm af4 system - by Bioz Stars, 2026-06
    86/100 stars
    		  Buy from Supplier
    af4 system af2000 tm  (Postnova Analytics)
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    Postnova Analytics af4 system af2000 tm
    Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique <t>(AF4).</t> (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.
    Af4 System Af2000 Tm, supplied by Postnova Analytics, 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/result/af4 system af2000 tm/product/Postnova Analytics
    Average 86 stars, based on 1 article reviews
    af4 system af2000 tm - by Bioz Stars, 2026-06
    86/100 stars
    		  Buy from Supplier

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    Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique (AF4). (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.

    Journal: Small (Weinheim an Der Bergstrasse, Germany)

    Article Title: Thermo‐Chemically Modified Silk Scaffolds Reveal Niche‐Driven Regulation of Hematopoiesis and Fibrosis

    doi: 10.1002/smll.202513071

    Figure Lengend Snippet: Structural and rheological characterization of silk fibroin variants. (a) Schematic overview of silk fibroin (SF) processing from Bombyx mori cocoons. Key steps include degumming at different timings (10, 30, 50 min) to remove sericin, dissolution and dialysis, and recovery to obtain silk fibroin solutions with varying molecular weights. (b) Structural depiction of SF10, SF30, and SF50 proteins, highlighting their secondary structure organization as determined by degumming time. Increasing degumming time correlates with increased fragmentation and reduced molecular weight. (c—I) Weight‐average molar mass ( M w ¯ ) versus radius of gyration ( R g ) of SF10, SF30, and SF50 obtained via asymmetric flow field‐flow fractionation technique (AF4). (c—II) Correlation between R g and hydrodynamics radius ( R h ) of SF10, SF30, and SF50 (left axis) and shape factor ( R g / R h ). (d—I) β‐sheet and α‐helix fractions (areas of peaks at ∼ 1515 and ∼ 1545 cm −1 (from Gaussian fittings) divided by the total area of the amide II band) and crystallinity index (CI; from the 1515/1545 cm −1 absorbance ratio). Please note that here we have employed the amide II rather than the possibly more common amide I band; the former is equally informative about protein secondary structures , and indeed the two bands provide rather similar information , but the former is advantageous for fully hydrated samples like ours, because it does not suffer from interference with the water bending (δOH) absorption. (d—II) Schematic representation of silk fibroin crystalline domain. (e) tan (δ) of 0.2% % wt. SF10, SF30, and SF50 as a function of frequency (ω) obtained from diffusing wave spectroscopy (DWS). Please refer to Figure , for the dependency on concentration in the 0.1–4.0% range. (f) Correlation plot describing the effect of degumming‐time‐dependent degradation and denaturation process on SF10, SF30, and SF50 structural properties.

    Article Snippet: 3 mg mL −1 SF10, SF30, or SF50 solutions in 1.0 mM LiBr were analyzed using an AF2000 TM AF4 System (Postnova Analytics, Landsberg, Germany) coupled to a PN3210 UV/Vis detector working at a wavelength of 220 Nm (Shimadzu SPD‐20A, Postnova Analytics), and a Dawn Heleos II Multi‐angle Light Scattering (MALS) (Wyatt Technology, Santa Barbara, California) working at a wavelength of 660 Nm and a Optilab T‐rEX refractive index (RI) (Wyatt Technology) detector in the given order.

    Techniques: Dissolution, Molecular Weight, Field Flow Fractionation, Spectroscopy, Concentration Assay