Review





Similar Products

talos-150 667- n thrusters  (Astrobotic Technology Inc)
90
Astrobotic Technology Inc talos-150 667- n thrusters
Talos 150 667 N Thrusters, supplied by Astrobotic Technology 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/product/talos+n/talos+150+667++n+thrusters/10__3847_slash_psj_slash_ad9927-72-9-35
Average 90 stars, based on 1 article reviews
talos-150 667- n thrusters - by Bioz Stars, 2026-10
90/100 stars
  Buy from Supplier
talos n  (Bruker Corporation)
99
Bruker Corporation talos n
Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
Talos N, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/talos+n/TopSpin+Software/pm39579771-224-119-127
Average 99 stars, based on 1 article reviews
talos n - by Bioz Stars, 2026-10
99/100 stars
  Buy from Supplier
talos-n software  (Federation of European Neuroscience Societies)
90
Federation of European Neuroscience Societies talos-n software
Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
Talos N Software, supplied by Federation of European Neuroscience Societies, 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/talos+n/talos+n+software/pm36282120-57-7-25
Average 90 stars, based on 1 article reviews
talos-n software - by Bioz Stars, 2026-10
90/100 stars
  Buy from Supplier
n a talos 120 transmission electron microscope  (Thermo Fisher)
86
Thermo Fisher n a talos 120 transmission electron microscope
Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
N A Talos 120 Transmission Electron Microscope, supplied by Thermo Fisher, 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/product/talos+n/pm35081340-234-228-236
Average 86 stars, based on 1 article reviews
n a talos 120 transmission electron microscope - by Bioz Stars, 2026-10
86/100 stars
  Buy from Supplier
program talos-n  (Biomol GmbH)
90
Biomol GmbH program talos-n
Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
Program Talos N, supplied by Biomol GmbH, 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/talos+n/talos/us10851139-30-12-19
Average 90 stars, based on 1 article reviews
program talos-n - by Bioz Stars, 2026-10
90/100 stars
  Buy from Supplier
purchase talos n software  (Bruker Corporation)
99
Bruker Corporation purchase talos n software
Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) <t>The</t> <t>TALOS-N</t> secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.
Purchase Talos N Software, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/talos+n/pmc05705324__NIHMS74110___supplement___Reporting_Summary-29-10-28
Average 99 stars, based on 1 article reviews
purchase talos n software - by Bioz Stars, 2026-10
99/100 stars
  Buy from Supplier

Image Search Results


Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) The TALOS-N secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.

Journal: Structure (London, England : 1993)

Article Title: The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail.

doi: 10.1016/j.str.2024.10.031

Figure Lengend Snippet: Figure 3. NMR analysis of KKT23125–348 structure and dynamics (A) The TALOS-N secondary structure analysis of KKT23125348 shows a mixed a/b topology. The secondary structure elements for which the probability was lower than 0.5 are not shown in the figure. See also Data S2. (B) The secondary structure elements identified using TALOS-N (A) are highlighted in the crystal structure of KKT23125348 showing a good agreement between the two methods. The b-strands and a-helices are colored in red and blue, respectively. See also Figure S4 and Data S2. (C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops. The {1H}-15N hetNOE errors were estimated from 500 Monte Carlo simulations using baseline noise as a measure of peak height error.

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER ASTRA Wyatt Technology https://store.wyatt.com/shop/ viscostar/viscostar-iii/astra-software/ BUCCANEER (Cowtan et al.)49 http://www.ccp4.ac.uk/ CCPNmr (Vranken et al.)50 https://www.ccpn.ac.uk COOT (Emsley et al.)51 http://www2.mrc-lmb.cam.ac.uk/ Personal/pemsley/coot/ CRANK2 (Skubak et al.)52 http://www.ccp4.ac.uk/ DALI server (Holm)19 http://ekhidna2.biocenter.helsinki.fi/dali/ Diffraction Anisotropy Server (Strong et al.)53 http://services.mbi.ucla.edu/anisoscale/ DisEMBL (Linding et al.)54 http://dis.embl.de Foldseek (van Kempen et al.)20 https://github.com/steineggerlab/foldseek HMMER web server (Potter et al.)55 https://www.ebi.ac.uk/Tools/hmmer/ ImageJ (Schneider et al.)56 https://imagej.net Jalview (Waterhouse et al.)57 http://www.jalview.org/ MAFFT (Katoh et al.)58 https://mafft.cbrc.jp/alignment/server/ MaxQuant (Cox and Mann)59 https://www.maxquant.org/ NMRPipe (Delaglio et al.)60 https://spin.niddk.nih.gov/NMRPipe/ PHASER (McCoy et al.)61 http://www.ccp4.ac.uk/ PHENIX (Liebschner et al.)62 http://www.phenix-online.org/ pLink2 (Chen et al.)63 https://www.cog-genomics.org/plink/2.0/ PRIDE database (Perez-Riverol et al.)64 http://www.proteomexchange.org PyMOL (DeLano et al.)14 http://www.pymol.org/ SEDFIT (Schuck et al.)65 https://sedfitsedphat.github.io/ SEDNTERP (Hayes)66 http://www.jphilo.mailway.com/index.htm TALOS-N (Shen et al.)17 https://spin.niddk.nih.gov/bax/ software/TALOS-N/ TOPSPIN 3.2 Bruker Biospin https://www.bruker.com/service/ support-upgrades/softwaredownloads/nmr.html TriTryp database (Aslett et al.)67 https://tritrypdb.org UniProt (UniProt)68 https://www.uniprot.org xiView (Graham et al.)69 https://xiview.org/index.php

Techniques: Sequencing