Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology
Author:
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s10858-007-9166-6.pdf
Reference57 articles.
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2. Asakawa N, Kuroki S, Kurosu H, Ando I, Shoji A, Ozaki T (1992) Hydrogen-bonding effect on 13C NMR chemical shifts of L-Alanine residue carbonyl carbons of peptides in the solid state. J Am Chem Soc 114:3261–3265
3. Avbelj F, Kocjan D, Baldwin RL (2004) Protein chemical shifts arising from α-helices and β-sheets depend on solvent exposure. Proc Natl Acad Sci USA 101:17394–17397
4. Bartels C, Billeter M, Güntert P, Wüthrich K (1996) Automated sequence-specific NMR assignment of homologous proteins using the program GARANT. J Biomol NMR 7:207–213
5. Beger RD, Bolton PH (1997) Protein ϕ and ψ dihedral restraints determined from multidimensional hypersurface correlations of backbone chemical shifts and their use in the determination of protein tertiary structures. J Biomol NMR 10:129–142
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