NMR Hydrogen Exchange of the OB-fold Protein LysN as a Function of Denaturant: The Most Conserved Elements of Structure are the Most Stable to Unfolding

By Alexandrescu A.T.   Jaravine V.A.   Dames S.A.   Lamour F.P.  

Journal of Molecular Biology, Vol. 289, Iss. 4, 1999-06 ,pp. : 1041-1054

Academic Press

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Conformational Analysis of a Set of Peptides Corresponding to the Entire Primary Sequence of the N-terminal Domain of the Ribosomal Protein L9: Evidence for Stable Native-like Secondary Structure in the Unfolded State

By Luisi D.L.   Wu W-J.   Raleigh D.P.  

Journal of Molecular Biology, Vol. 287, Iss. 2, 1999-03 ,pp. : 395-407

Academic Press

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Native-like &bgr;-Hairpin Retained in the Cold-denatured State of Bovine &bgr;-Lactoglobulin

By Katou H.   Hoshino M.   Kamikubo H.   Batt C.A.   Goto Y.  

Journal of Molecular Biology, Vol. 310, Iss. 2, 2001-07 ,pp. : 471-484

Academic Press

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Biophysical Characterization of a Soluble CD40 Ligand (CD154) Coiled-Coil Trimer: Evidence of a Reversible Acid-Denatured Molten Globule

By Matsuura J.E.   Morris A.E.   Ketchem R.R.   Braswell E.H.   Klinke R.   Gombotz W.R.   Remmele R.L.  

Archives of Biochemistry and Biophysics, Vol. 392, Iss. 2, 2001-08 ,pp. : 208-218

Elsevier

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Generation of native-like protein structures from limited NMR data, modern force fields and advanced conformational sampling

By Chen Jianhan   Won Hyung-Sik   Im Wonpil   Dyson H.   Brooks Charles  

Journal of Biomolecular NMR, Vol. 31, Iss. 1, 2005-01 ,pp. : 59-64

Springer Publishing Company

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