References

Found 8 results
Author [ Title(Desc)] Type Year
Filters: Author is Lange, Oliver F  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
B
[Rosato2012a] Rosato A, Aramini JM, Arrowsmith C, Bagaria A, Baker D, Cavalli A, Doreleijers JF, Eletsky A, Giachetti A, Guerry P et al..  2012.  Blind testing of routine, fully automated determination of protein structures from NMR data.. Structure. 20(2):227-236.
C
[shen2008a] Shen Y, Lange OF, Delaglio F, Rossi P, Aramini JM, Liu G, Eletsky A, Wu Y, Singarapu KK, Lemak A et al..  2008.  Consistent blind protein structure generation from NMR chemical shift data.. P. Natl. Acad. Sci. USA. 105(12):4685-4690.
D
[Lange2012b] Lange OF, Rossi P, Sgourakis NG, Song Y, Lee H-W, Aramini JM, Ertekin A, Xiao R, Acton TB, Montelione GT et al..  2012.  Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples. Proc Nat Am Soc. (in press)
[Sgourakis2011a] Sgourakis NG, Lange OF, DiMaio F, Andre I, Fitzkee NC, Rossi P, Montelione GT, Bax A, Baker D.  2011.  Determination of the structures of symmetric protein oligomers from NMR chemical shifts and residual dipolar couplings.. J. Am. Chem. Soc.. 133(16):6288-6298.
N
[raman2010a] Raman S, Lange OF, Rossi P, Tyka M, Wang X, Aramini JM, Liu G, Ramelot TA, Eletsky A, Szyperski T et al..  2010.  NMR structure determination for larger proteins using backbone-only data.. Science. 327(5968):1014-1018.
R
[Lange2012a] Lange OF, Baker D.  2012.  Resolution-adapted recombination of structural features significantly improves sampling in restraint-guided structure calculation.. Proteins. 80(3):884-895.
S
[Bouvignies2011a] Bouvignies G, Vallurupalli P, Hansen FD, Correia BE, Lange OF, Bah A, Vernon R, Dahlquist FW, Baker D, Kay LE.  2011.  Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.. Nature. 477(7362):111-114.
[Warner2011a] Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A.  2011.  Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set.. J Mol Biol. 411(1):83-95.