Andrew Lee

Home > Faculty & Research > Faculty Directory
Document Actions

Igumenova, T.I., Lee, A.L., and Wand, A.J.  Backbone and side chain dynamics of mutant calmodulin-peptide complexes.  Biochemistry (2005), 44, 12627-12639.

Bryant, J.E., Lecomte, J.T.J., Lee, A.L., Young, G.B., and Pielak, G.J.  Protein dynamics in living cells.  Biochemistry (2005), 44, 9275-9279.

Hu, H., Hermans, J., and Lee, A.L.  Relating side-chain mobility in proteins to rotameric transitions:  Insights from molecular dynamics simulations and NMR.  J. Biomol. NMR (2005), 32, 151-162.

Partch, C.L., Clarkson, M.W., Ozgur, S., Lee, A.L., and Sancar, A.  Role of structural plasticity in signal transduction of the cryptochrome blue-light photoreceptor.  Biochemistry (2005) 44, 3795-3805.

Clarkson, M.W. and Lee, A.L.  Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c.  Biochemistry (2004) 43, 12448-12458.

Ohnishi, S., Lee, A.L., Edgell, M.H., and Shortle, D.: Direct Demonstration of Structural Similarity Between Native and Denatured Eglin C. Biochemistry (2004) 43, 4064-4070.

Fuentes, E.J., Der, C.J., and Lee, A.L.  Ligand-Dependent Dynamics and Intramolecular Signaling in a PDZ Domain.  J. Mol. Biol. (2004), 335, 1105-1115.

Hu, H., Clarkson, M.W., Hermans, J., and Lee, A.L.  Increased Rigidity of Eglin c at Acidic pH:  Evidence from NMR Spin-Relaxation and MD Simulations.  Biochemistry (2003), 42, 13856-13868.

Prabhu, N.V., Lee, A.L., Wand, A.J., and Sharp, K.A.  Dynamics and Entropy of a Calmodulin-Peptide Complex Studied by NMR and Molecular Dynamics.  Biochemistry (2003), 42, 562-570.

Lee, A.L., Sharp, K.A., Kranz, J.K., Song, X., and Wand, A.J.  Temperature Dependence of the Internal Dynamics of a Calmodulin-Peptide Complex.  Biochemistry (2002), 41, 13814-13825.

Walsh, S.T.R., Lee, A.L., DeGrado, W.F., and Wand, A.J.  Backbone and Side-Chain Dynamics of a De novo Designed Three-Helix Bundle Protein Studied by 15N, 13C, and 2H NMR Relaxation Methods.  Biochemistry (2001), 40, 9560-9569.

Flynn, P.F., Urbauer, R.J.B., Zhang, H., Lee, A.L., and Wand, A.J.  Main Chain and Side Chain Dynamics of a Heme Protein: 15N and 2H NMR Relaxation Studies of R. capsulatus Ferrocytochrome c2.  Biochemistry (2001), 40, 6559-6569.

Lee, A.L. and Wand, A.J.  Microscopic Origins of Entropy, Heat Capacity and the Apparent Glass Transition in Proteins:  The Internal Dynamics of a Calmodulin-Peptide Complex.  Nature (2001), 411, 501-504.

Lee, A.L., Kinnear, S.A., and Wand, A.J.  Redistribution and Loss of Side-Chain Entropy Upon Formation of a Calmodulin-Peptide Complex.  Nat. Struct. Biol. (2000) 7, 72-77.

Volkman, B.F., Wilkens, S.J., Lee, A.L., Xia, B., Westler, W.W., Beger, R., and Markley, J.L.  Redox-dependent Magnetic Alignment of Clostridium pasteurianum Rubredoxin:  Measurement of Magnetic Susceptibility Anisotropy and Prediction of Pseudocontact Shift Contributions.  J. Am. Chem. Soc. (1999) 121, 4677-4683.

Lee, A.L., Flynn, P.F., and Wand, A.J.  Comparison of 2H and 13C Relaxation Techniques for the Study of Protein Methyl Group Dynamics in Solution.  J. Am. Chem. Soc. (1999) 121, 2891-2902.

Lee, A.L. and Wand, A.J.  Assessing Potential Bias in the Determination of Rotational Correlation Times of Proteins by NMR Relaxation.  J. Biomol. NMR (1999) 13, 101-112.

Lee, A.L., Urbauer, J.L., and Wand, A.J.  Improved Labeling Strategy for 13C Relaxation Measurements of Methyl Groups in Proteins.  J. Biomol. NMR (1997) 9, 437-440.

Lee, A.L., Volkman, B.F., Robertson, S.A., Rudner, D.Z., Barbash, D.A., Cline, T.W., Kanaar, R., Rio, D.C., and Wemmer, D.E.  Chemical Shift Mapping of the RNA-Binding Interface of the Multiple-RBD Protein Sex-lethal.  Biochemistry (1997) 36, 14306-14317.

Kanaar, R., Lee, A.L., Rudner, D.Z., Wemmer, D.E. , and Rio, D.C.  Interaction of the Sex-lethal RNA Binding Domains with RNA.  EMBO J. (1995) 14, 4530-4539.

Lee, A.L., Kanaar, R., Rio, D.C., and Wemmer, D.E.  Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-Lethal Determined by Multidimensional Heteronuclear Magnetic Resonance.  Biochemistry (1994) 33, 13775-13786.