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Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
Cell 10K protein) (CC10) (CC16) Ceruloplasmin isoforms Chain A, Crystal structure of novel mammalian lectin Ym1-suggests a saccharide binding site Chain B, Chimeric human mouse carbonmonoxyhemoglobin (Human zeta, Mouse beta 2) Chia protein Coiled-coil domain containing 122 Complement component 3 Complement component C5 Contrapsin (Serine protease inhibitor A3K) Creatine kinase M-type (EC.2.7.3.2)
10.69 4.76 12.73 29.21 31.75 38.77 16.63 -12.1 2 3 4 5 6 714-3-3-Zeta Adipsin (Complement factor D) Albumin Aldehyde dehydrogenase AHD-M1 Aldehyde dehydrogenase II Aldehyde dehydrogenase, Dimeric NADP-preferring (EC 1.2.1.5) (ALDH class 3) Alpha-1-antitrypsin 1-1 precursor (Serine protease inhibitor 1-1) Alpha-1-antitrypsin 1-6 precursor (Serine protease inhibitor 1-6) (Alpha-1 protease inhibitor
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
N of a -sheet using strands from the two monomers. As expected, CS-Rosetta calculations of the individual monomers failed to converge (Figure 5A); the native state cannot be energetically distinguished by considering only interactions within the monomer. If nevertheless the low energy, partially unfolded monomers are used as starting points in the symmetric docking protocol we obtain a converged
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya
Ntrol, 4 hr post infection and 24 hr post infection: percent changes with significance for all identified proteins corresponding to reference gels in Fig. 2 (Continued)33 34 35 36 37 38 39 40 Glutathione S-transferase, alpha 3 Glutathione S-transferase, alpha 4 Glutathione S-transferase, mu 1 Glutathione S-transferase, omega 1 (Similar to) Glutathione S-transferase, Ya chain (GST class-alpha) (Ya