Main-chain Dynamics of a Partially Folded Protein: N NMR Relaxation Measurements of Hen Egg White Lysozyme Denatured in Trifluoroethanol

By Buck M.   Schwalbe H.   Dobson C.M.  

Journal of Molecular Biology, Vol. 257, Iss. 3, 1996-04 ,pp. : 669-683

Academic Press

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A suite of Mathematica notebooks for the analysis of protein main chain ¹⁵N NMR relaxation data

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Journal of Biomolecular NMR, Vol. 36, Iss. 4, 2006-12 ,pp. : 215-224

Springer Publishing Company

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Role of Main-chain Electrostatics, Hydrophobic Effect and Side-chain Conformational Entropy in Determining the Secondary Structure of Proteins

By Avbelj F.   Fele L.  

Journal of Molecular Biology, Vol. 279, Iss. 3, 1998-06 ,pp. : 665-684

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The Conformations of Polypeptide Chains Where the Main-chain Parts of Successive Residues are Enantiomeric. Their Occurrence in Cation and Anion-binding Regions of Proteins

By Watson J.D.   Milner-White E.J.  

Journal of Molecular Biology, Vol. 315, Iss. 2, 2002-01 ,pp. : 183-191

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Side-chain Conformations in an Unfolded Protein: &khgr;₁Distributions in Denatured Hen Lysozyme Determined by Heteronuclear¹³C,¹⁵N NMR Spectroscopy

By Hennig M.   Bermel W.   Spencer A.   Dobson C.M.   Smith L.J.   Schwalbe H.  

Journal of Molecular Biology, Vol. 288, Iss. 4, 1999-05 ,pp. : 705-723

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