Stereospecific assignment of the asparagine and glutamine sidechain amide protons in proteins from chemical shift analysis
Author:
Funder
VCI
HFSPO
DFG
Alexander von Humboldt-Stiftung
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s10858-017-0093-x.pdf
Reference17 articles.
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2. Bundi A, Wuthrich K (1979) 1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 18:285–297
3. Gronwald W, Kalbitzer HR (2004) Automated structure determination of proteins by NMR spectroscopy. Prog Nucl Magn Reson Spectrosc 44:33–96
4. Harsch T, Dasch C, Donaubauer H, Baskaran K, Kremer W, Kalbitzer HR (2013) Stereospecific assignment of the asparagine and glutamine side chain amide protons in random-coil peptides by combination of molecular dynamic simulations with relaxation matrix calculations. Appl Magn Reson 44(1–2):319–331
5. Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3):435–447
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