Russell R, Fritz M, Kraus J, Quinn C, Polenova T, Gronenborn A
J Biomol NMR. 2019; 73(6-7):333-346.
PMID: 30847635
PMC: 6693955.
DOI: 10.1007/s10858-019-00233-9.
Hafsa N, Berjanskii M, Arndt D, Wishart D
J Biomol NMR. 2017; 70(1):33-51.
PMID: 29196969
DOI: 10.1007/s10858-017-0154-1.
Schwieters C, Bermejo G, Clore G
Protein Sci. 2017; 27(1):26-40.
PMID: 28766807
PMC: 5734396.
DOI: 10.1002/pro.3248.
Fenwick R, Oyen D, Wright P
Phys Chem Chem Phys. 2015; 18(8):5789-98.
PMID: 26426424
PMC: 4758882.
DOI: 10.1039/c5cp04670j.
Kaczka P, Winiewska M, Zhukov I, Rempola B, Bolewska K, Lozinski T
Eur Biophys J. 2014; 43(12):581-94.
PMID: 25261014
PMC: 4236625.
DOI: 10.1007/s00249-014-0987-4.
A NMR experiment for simultaneous correlations of valine and leucine/isoleucine methyls with carbonyl chemical shifts in proteins.
Tugarinov V, Venditti V, Clore G
J Biomol NMR. 2013; 58(1):1-8.
PMID: 24346684
PMC: 3974575.
DOI: 10.1007/s10858-013-9803-1.
Serverification of molecular modeling applications: the Rosetta Online Server that Includes Everyone (ROSIE).
Lyskov S, Chou F, Conchuir S, Der B, Drew K, Kuroda D
PLoS One. 2013; 8(5):e63906.
PMID: 23717507
PMC: 3661552.
DOI: 10.1371/journal.pone.0063906.
Analysis of (1)H chemical shifts in DNA: Assessment of the reliability of (1)H chemical shift calculations for use in structure refinement.
Wijmenga S, Kruithof M, Hilbers C
J Biomol NMR. 2010; 10(4):337-50.
PMID: 20859781
DOI: 10.1023/A:1018348123074.
Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.
Saito H, Ando I, Ramamoorthy A
Prog Nucl Magn Reson Spectrosc. 2010; 57(2):181-228.
PMID: 20633363
PMC: 2905606.
DOI: 10.1016/j.pnmrs.2010.04.005.
4D prediction of protein (1)H chemical shifts.
Lehtivarjo J, Hassinen T, Korhonen S, Perakyla M, Laatikainen R
J Biomol NMR. 2009; 45(4):413-26.
PMID: 19876601
DOI: 10.1007/s10858-009-9384-1.
Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations.
Wilton D, Kitahara R, Akasaka K, Pandya M, Williamson M
Biophys J. 2009; 97(5):1482-90.
PMID: 19720037
PMC: 2749754.
DOI: 10.1016/j.bpj.2009.06.022.
Dependence of amino acid side chain 13C shifts on dihedral angle: application to conformational analysis.
London R, Wingad B, Mueller G
J Am Chem Soc. 2008; 130(33):11097-105.
PMID: 18652454
PMC: 2712834.
DOI: 10.1021/ja802729t.
Definition of a new information-based per-residue quality parameter.
Nabuurs S, Krieger E, Spronk C, Nederveen A, Vriend G, Vuister G
J Biomol NMR. 2005; 33(2):123-34.
PMID: 16258830
DOI: 10.1007/s10858-005-2826-5.
Secondary structural effects on protein NMR chemical shifts.
Wang Y
J Biomol NMR. 2005; 30(3):233-44.
PMID: 15754052
DOI: 10.1007/s10858-004-3098-1.
An evaluation of chemical shift index-based secondary structure determination in proteins: influence of random coil chemical shifts.
Mielke S, Krishnan V
J Biomol NMR. 2005; 30(2):143-53.
PMID: 15666561
DOI: 10.1023/b:jnmr.0000048940.51331.49.
The solution structure of bovine pancreatic trypsin inhibitor at high pressure.
Williamson M, Akasaka K, Refaee M
Protein Sci. 2003; 12(9):1971-9.
PMID: 12930996
PMC: 2323994.
DOI: 10.1110/ps.0242103.
Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts.
Neal S, Nip A, Zhang H, Wishart D
J Biomol NMR. 2003; 26(3):215-40.
PMID: 12766419
DOI: 10.1023/a:1023812930288.
Prediction of proton chemical shifts in RNA. Their use in structure refinement and validation.
Cromsigt J, Hilbers C, Wijmenga S
J Biomol NMR. 2001; 21(1):11-29.
PMID: 11693565
DOI: 10.1023/a:1011914132531.
Pressure-dependent changes in the structure of the melittin alpha-helix determined by NMR.
Iwadate M, Asakura T, Dubovskii P, Yamada H, Akasaka K, Williamson M
J Biomol NMR. 2001; 19(2):115-24.
PMID: 11256808
DOI: 10.1023/a:1008392327013.
RESCUE: an artificial neural network tool for the NMR spectral assignment of proteins.
Pons J, Delsuc M
J Biomol NMR. 1999; 15(1):15-26.
PMID: 10549132
DOI: 10.1023/a:1008338605320.
