interactive molecular dynamics flexible fitting tools Search Results


dynamics flexible fitting (mdff) plugin for namd 2.8  (Molecular Dynamics Inc)
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Molecular Dynamics Inc dynamics flexible fitting (mdff) plugin for namd 2.8
Dynamics Flexible Fitting (Mdff) Plugin For Namd 2.8, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dynamics flexible fitting (mdff)  (Molecular Dynamics Inc)
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Molecular Dynamics Inc dynamics flexible fitting (mdff)
Dynamics Flexible Fitting (Mdff), supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dynamics flexible fitting (mdff) - by Bioz Stars, 2026-04
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dynamics flexible fitting simulation  (Molecular Dynamics Inc)
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Molecular Dynamics Inc dynamics flexible fitting simulation
Dynamics Flexible Fitting Simulation, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dynamics flexible fitting simulation - by Bioz Stars, 2026-04
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dynamics flexible fit (mdff)  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc dynamics flexible fit (mdff)
Dynamics Flexible Fit (Mdff), supplied by Molecular Dynamics Inc, 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/result/dynamics flexible fit (mdff)/product/Molecular Dynamics Inc
Average 90 stars, based on 1 article reviews
dynamics flexible fit (mdff) - by Bioz Stars, 2026-04
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interactive molecular dynamics flexible fitting tools  (Molecular Dynamics Inc)
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Molecular Dynamics Inc interactive molecular dynamics flexible fitting tools
Interactive Molecular Dynamics Flexible Fitting Tools, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
interactive molecular dynamics flexible fitting tools - by Bioz Stars, 2026-04
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dynamics flexible fitting protocol  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc dynamics flexible fitting protocol
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Dynamics Flexible Fitting Protocol, supplied by Molecular Dynamics Inc, 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/result/dynamics flexible fitting protocol/product/Molecular Dynamics Inc
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dynamics flexible fitting protocol - by Bioz Stars, 2026-04
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mdff (molecular dynamics flexible fitting)  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc mdff (molecular dynamics flexible fitting)
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Mdff (Molecular Dynamics Flexible Fitting), supplied by Molecular Dynamics Inc, 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/result/mdff (molecular dynamics flexible fitting)/product/Molecular Dynamics Inc
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dynamics flexible fitting simulation of a light harvesting protein  (Molecular Dynamics Inc)
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Molecular Dynamics Inc dynamics flexible fitting simulation of a light harvesting protein
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Dynamics Flexible Fitting Simulation Of A Light Harvesting Protein, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dynamics flexible fitting simulation of a light harvesting protein - by Bioz Stars, 2026-04
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namdinator molecular dynamics flexible fitting  (Molecular Dynamics Inc)
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Molecular Dynamics Inc namdinator molecular dynamics flexible fitting
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Namdinator Molecular Dynamics Flexible Fitting, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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namdinator molecular dynamics flexible fitting - by Bioz Stars, 2026-04
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dynamics flexible fitting cross correlation  (Molecular Dynamics Inc)
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Molecular Dynamics Inc dynamics flexible fitting cross correlation
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Dynamics Flexible Fitting Cross Correlation, supplied by Molecular Dynamics Inc, 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/result/dynamics flexible fitting cross correlation/product/Molecular Dynamics Inc
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dynamics flexible fitting cross correlation - by Bioz Stars, 2026-04
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flexible fitting  (Molecular Dynamics Inc)
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Molecular Dynamics Inc flexible fitting
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Flexible Fitting, supplied by Molecular Dynamics Inc, 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/result/flexible fitting/product/Molecular Dynamics Inc
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cascade molecular dynamics flexible fitting  (Molecular Dynamics Inc)
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Molecular Dynamics Inc cascade molecular dynamics flexible fitting
Comparison of the domain organization of E. coli <t>IF2</t> and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.
Cascade Molecular Dynamics Flexible Fitting, supplied by Molecular Dynamics Inc, 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/result/cascade molecular dynamics flexible fitting/product/Molecular Dynamics Inc
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Image Search Results


Comparison of the domain organization of E. coli IF2 and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Article Title: Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1

doi: 10.1073/pnas.1017425108

Figure Lengend Snippet: Comparison of the domain organization of E. coli IF2 and mammalian IF2mt, and cryo-EM structure of the complex. (A) Domain alignment of E. coli IF2 and bovine IF2mt. Note that the mature IF2mt (i.e., after deletion of the import sequence) starts from aa residue 78. The 37-aa insertion in IF2mt is highlighted in red. (B) The cryo-EM map of the E. coli 70S ribosome (30S subunit, yellow; 50S subunit, blue) in complex with IF2mt (red), initiator tRNA (green) at the P/I position, and an additional tRNA density (brown, visible in panels C and D) at the ribosomal E site. (C and D) The 30S and 50S subunit portions of the map are shown from their interface sides to reveal the overall binding positions of IF2mt and tRNAs. Landmarks of the 30S subunit: h, head; sh, shoulder; b, body; and pt, platform. Landmarks of the 50S subunit: L1, L1 protein protuberance; CP, central protuberance; and Sb, L7/L12 stalk base. For stereo viewing, see Fig. S2.

Article Snippet: The final atomic model of IF2 mt was obtained by flexible fitting into the cryo-EM density corresponding to IF2 mt ( ) using the Molecular Dynamics Flexible Fitting (MDFF) protocol ( 34 ).

Techniques: Comparison, Cryo-EM Sample Prep, Sequencing, Residue, Binding Assay