✦ LIBER ✦

GFT NMR based resonance assignment for the 21 kDa human protein UFC1

✍ Scribed by Gaohua Liu; James Aramini; Hanudatta S. Atreya; Alexander Eletsky; Rong Xiao; Thomas Acton; LiChung Ma; Gaetano T. Montelione; Thomas Szyperski

Publisher: Springer Netherlands
Year: 2005
Tongue: English
Weight: 150 KB
Volume: 32
Category: Article
ISSN: 0925-2738
DOI: 10.1007/s10858-005-7941-9

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

NMR resonance assignments of the human h

NMR resonance assignments of the human high mobility group protein HMGA1

✍ Garry W. Buchko; Shuisong Ni; Natacha M. Lourette; Raymond Reeves; Michael A. Ke 📂 Article 📅 2007 🏛 Springer Netherlands 🌐 English ⚖ 83 KB

Assignment of the gene for human spasmol

Assignment of the gene for human spasmolytic protein (hSP/SML1) to chromosome 21

✍ Birgit Theisinger; Cornelius Welter; Karl-Heinz Grzeschik; Nikolaus Blin 📂 Article 📅 1992 🏛 Springer 🌐 English ⚖ 186 KB

A human cDNA corresponding to the porcine pancreatic spasmolytic protein (PSP) was isolated, and the recombinant clone was originally termed hSP for human spasmolytic protein. Later, the term SML1 for spasmolysin was suggested for the human gene. This protein shows a remarkable sequence homology to

Solution NMR Studies of an Intrinsically

Solution NMR Studies of an Intrinsically Unstructured Protein within a Dilute, 75 kDa Eukaryotic Protein Assembly; Probing the Practical Limits for Efficiently Assigning Polypeptide Backbone Resonances

✍ Yuefeng Wang; Igor Filippov; Christian Richter; Rensheng Luo; Richard W. Kriwack 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 470 KB

An1H–13C–13C-Edited1H NMR Experiment for

An1H–13C–13C-Edited1H NMR Experiment for Making Resonance Assignments in the Active Site of Heme Proteins

✍ Feng Qiu; Mario Rivera; Ruth E. Stark 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 159 KB

In paramagnetic heme proteins, it is often problematic to make the reduced (usually diamagnetic) state lack isotropic shifts proton resonance assignments for heme substituents that do not and are therefore difficult to examine by NMR spectroscopy. have large isotropic shifts and consequently lie und

3D13C/1H NMR-based assignments for side-

3D13C/1H NMR-based assignments for side-chain resonances ofLactobacillus caseidihydrofolate reductase. Evidence for similarities between the solution and crystal structures of the enzyme

✍ A. Soteriou; M. D. Carr; T. A. Frenkiel; J. E. McCormick; C. J. Bauer; D. Šali; 📂 Article 📅 1993 🏛 Springer Netherlands 🌐 English ⚖ 731 KB

~3C-based three-dimensional 1H-1H correlation experiments have been used to determine essentially complete 13C and 1H resonance assignments for the amino acid side chains of uniformly 13C/15N labelled L. casei dihydrofolate reductase in a complex with the drug methotrexate. Excellent agreement is ob

New 15N NMR Exchange Experiments for the

New 15N NMR Exchange Experiments for the Unambiguous Assignment of 1HN/15N Resonances of Proteins in Complexes in Slow Chemical Exchange with Free Form

✍ Catherine Vialle-Printems; Carine van Heijenoort; Eric Guittet 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 120 KB

The potentialities of a 2D proton-detected heteronuclear exchange experiment to assign the nitrogen and amide proton resonances in a uniformly 15 N-enriched macromolecule involved in a complex, starting from the free form assignments, are demonstrated on a protein-DNA complex. This 2D experiment is