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cold sam  (New England Biolabs)


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    Structured Review

    New England Biolabs cold sam
    Definition of starting points for the development of S. <t>aureus</t> <t>TrmD</t> inhibitors. (A) Crystallographic overlay of literature-known inhibitors 1 (PDB: 4MCD ) and 2 (PDB: 4MCC ) in the H. influenzae <t>SAM-binding</t> pocket. Ligands and amino acids are shown in stick representation; polar interactions are shown as yellow lines, and water as red spheres. The carbon atoms of 1 are shown in pink and those of compound 2 in light green. Interacting residues are displayed in dark green. (B, C) Structures and affinities of inhibitors 1 (B) and 2 (C) binding to S. aureus TrmD determined by ITC, incl. thermograms, stoichiometry, and signature plots (data for H. influenzae TrmD in Figure S2 ). Due to low enthalpy signals, a low c -titration was performed for inhibitor 1 , resulting in N < 1.
    Cold Sam, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1462 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cold sam/product/New England Biolabs
    Average 96 stars, based on 1462 article reviews
    cold sam - by Bioz Stars, 2026-05
    96/100 stars

    Images

    1) Product Images from "Nanoscale Direct-to-Biology Optimization and Structural Insights into Selective S. aureus TrmD Inhibitors"

    Article Title: Nanoscale Direct-to-Biology Optimization and Structural Insights into Selective S. aureus TrmD Inhibitors

    Journal: Journal of Medicinal Chemistry

    doi: 10.1021/acs.jmedchem.5c02323

    Definition of starting points for the development of S. aureus TrmD inhibitors. (A) Crystallographic overlay of literature-known inhibitors 1 (PDB: 4MCD ) and 2 (PDB: 4MCC ) in the H. influenzae SAM-binding pocket. Ligands and amino acids are shown in stick representation; polar interactions are shown as yellow lines, and water as red spheres. The carbon atoms of 1 are shown in pink and those of compound 2 in light green. Interacting residues are displayed in dark green. (B, C) Structures and affinities of inhibitors 1 (B) and 2 (C) binding to S. aureus TrmD determined by ITC, incl. thermograms, stoichiometry, and signature plots (data for H. influenzae TrmD in Figure S2 ). Due to low enthalpy signals, a low c -titration was performed for inhibitor 1 , resulting in N < 1.
    Figure Legend Snippet: Definition of starting points for the development of S. aureus TrmD inhibitors. (A) Crystallographic overlay of literature-known inhibitors 1 (PDB: 4MCD ) and 2 (PDB: 4MCC ) in the H. influenzae SAM-binding pocket. Ligands and amino acids are shown in stick representation; polar interactions are shown as yellow lines, and water as red spheres. The carbon atoms of 1 are shown in pink and those of compound 2 in light green. Interacting residues are displayed in dark green. (B, C) Structures and affinities of inhibitors 1 (B) and 2 (C) binding to S. aureus TrmD determined by ITC, incl. thermograms, stoichiometry, and signature plots (data for H. influenzae TrmD in Figure S2 ). Due to low enthalpy signals, a low c -titration was performed for inhibitor 1 , resulting in N < 1.

    Techniques Used: Binding Assay, Titration



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    cold sam  (New England Biolabs)
    96
    New England Biolabs cold sam
    Definition of starting points for the development of S. <t>aureus</t> <t>TrmD</t> inhibitors. (A) Crystallographic overlay of literature-known inhibitors 1 (PDB: 4MCD ) and 2 (PDB: 4MCC ) in the H. influenzae <t>SAM-binding</t> pocket. Ligands and amino acids are shown in stick representation; polar interactions are shown as yellow lines, and water as red spheres. The carbon atoms of 1 are shown in pink and those of compound 2 in light green. Interacting residues are displayed in dark green. (B, C) Structures and affinities of inhibitors 1 (B) and 2 (C) binding to S. aureus TrmD determined by ITC, incl. thermograms, stoichiometry, and signature plots (data for H. influenzae TrmD in Figure S2 ). Due to low enthalpy signals, a low c -titration was performed for inhibitor 1 , resulting in N < 1.
    Cold Sam, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cold sam/product/New England Biolabs
    Average 96 stars, based on 1 article reviews
    cold sam - by Bioz Stars, 2026-05
    96/100 stars
    		  Buy from Supplier

    Image Search Results


    Definition of starting points for the development of S. aureus TrmD inhibitors. (A) Crystallographic overlay of literature-known inhibitors 1 (PDB: 4MCD ) and 2 (PDB: 4MCC ) in the H. influenzae SAM-binding pocket. Ligands and amino acids are shown in stick representation; polar interactions are shown as yellow lines, and water as red spheres. The carbon atoms of 1 are shown in pink and those of compound 2 in light green. Interacting residues are displayed in dark green. (B, C) Structures and affinities of inhibitors 1 (B) and 2 (C) binding to S. aureus TrmD determined by ITC, incl. thermograms, stoichiometry, and signature plots (data for H. influenzae TrmD in Figure S2 ). Due to low enthalpy signals, a low c -titration was performed for inhibitor 1 , resulting in N < 1.

    Journal: Journal of Medicinal Chemistry

    Article Title: Nanoscale Direct-to-Biology Optimization and Structural Insights into Selective S. aureus TrmD Inhibitors

    doi: 10.1021/acs.jmedchem.5c02323

    Figure Lengend Snippet: Definition of starting points for the development of S. aureus TrmD inhibitors. (A) Crystallographic overlay of literature-known inhibitors 1 (PDB: 4MCD ) and 2 (PDB: 4MCC ) in the H. influenzae SAM-binding pocket. Ligands and amino acids are shown in stick representation; polar interactions are shown as yellow lines, and water as red spheres. The carbon atoms of 1 are shown in pink and those of compound 2 in light green. Interacting residues are displayed in dark green. (B, C) Structures and affinities of inhibitors 1 (B) and 2 (C) binding to S. aureus TrmD determined by ITC, incl. thermograms, stoichiometry, and signature plots (data for H. influenzae TrmD in Figure S2 ). Due to low enthalpy signals, a low c -titration was performed for inhibitor 1 , resulting in N < 1.

    Article Snippet: The enzymatic reactions were started by the addition of SAM as a mixture of 3 H-SAM (Hartmann Analytics, S. aureus TrmD: 0.5 μM, Trm5: 2 μM) and cold SAM (New England Biolabs, S. aureus TrmD: 0.5 μM, Trm5: 98 μM) to a final activity of 0.04 μCi μL –1 (TrmD) or 0.16 μCi μL –1 (Trm5).

    Techniques: Binding Assay, Titration