Hello, I'm working on calculating a nmr structure of a protein using PRE data. Protein was labeled with MTSSL at 16 different places (each one at a time).PRE
NMR for a 30-residue peptide
Dear all,
Is that possible to do structure determination of a 30-residue peptide
using 500 MHz NMR?
I have a 30-residue linear peptide with three Gly and two AHx
(aminohexanoic acid) groups at the center of the peptide. I read some
papers from people who use 500 MHz NMR to determine the structure of
up to 20-residue peptides, but not a 30-residue peptide.
bimo
NMR Questions and Answers
5
03-06-2013 12:35 AM
[Question from NMRWiki Q&A forum] Side chain assignment of C-terminal residue
Side chain assignment of C-terminal residue
Dear Friends,
I am not able to figure out how to determine the side chain assignment of Last C-terminal SERINE residue of my protein. I can determine CA, CB, CO, N,H values from HNCA, CBCANH, HNCACO. Can someone tell which experiment will give me the information of HA, HB2 and HB3
Regards
Arun
nmrlearner
News from other NMR forums
0
10-09-2011 06:23 PM
[CNS Yahoo group] How to add bond between protein residue and a small molecule in CNS
How to add bond between protein residue and a small molecule in CNS
Dear All, I'm stuck in a step where in i need to connect a bond an amino acid residue and a small molecule in CNS Thank you. Joseph
More...
nmrlearner
News from other NMR forums
0
08-07-2011 01:35 AM
[NMR paper] 1H and 13C NMR investigation of the influence of nonligated residue contacts on the h
1H and 13C NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins.
Related Articles 1H and 13C NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins.
J Am Chem Soc. 2001 Oct 17;123(41):10063-70
Authors: Hu B, Hauksson JB, Tran AT, Kolczak U, Pandey RK, Rezzano IN, Smith KM, La Mar GN
...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Apoflavodoxin (un)folding followed at the residue level by NMR.
Apoflavodoxin (un)folding followed at the residue level by NMR.
Related Articles Apoflavodoxin (un)folding followed at the residue level by NMR.
Protein Sci. 2000 Jan;9(1):145-57
Authors: van Mierlo CP, van den Oever JM, Steensma E
The denaturant-induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR spectroscopy. NH groups of 21 residues of the protein could be followed in a series of 1H-15N heteronuclear single-quantum coherence spectra recorded at increasing concentrations of...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue s
Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus.
Related Articles Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus.
J Biomol NMR. 1995 Apr;5(3):259-70
Authors: Fogh RH, Schipper D, Boelens R, Kaptein R
The 1H, 13C and 15N NMR resonances of serine protease PB92 have been assigned using 3D triple-resonance NMR techniques. With a molecular weight of 27 kDa (269 residues) this...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p
1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus.
Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus.
J Biomol NMR. 1994 Mar;4(2):257-78
Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ
1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p
1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus.
Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus.
J Biomol NMR. 1994 Mar;4(2):257-78
Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ
1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...
MTSSL residue in CNS 1.2
Linear Mode
