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Computational design of a water-soluble analog of phospholamban
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A.M. Slovic, C.M. Summa, J.D. Lear, and W.F. DeGrado Computational design of a water-soluble analog of phospholamban Protein Sci 12 2003 337 348 The authors use a parameterized model structure for phospholamban and a residue-residue effective potential to identify a water-solubilized variant (WSPLB). WSPLB shares a number of experimentally determined properties with the wild-type membrane-soluble form: it is helical, possesses the same oligomerization state and is stabilized upon phosphorylation.
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(2003)
Protein Sci
, vol.12
, pp. 337-348
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Slovic, A.M.1
Summa, C.M.2
Lear3
Degrado, W.F.J.D.4
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54
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0345304457
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Computational design and characterization of a monomeric helical dinuclear metalloprotein
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J.R. Calhoun, H. Kono, S. Lahr, W. Wang, W.F. DeGrado, and J.G. Saven Computational design and characterization of a monomeric helical dinuclear metalloprotein J Mol Biol 334 2003 1101 1115 The de novo design of structure, sequence and function for a 114-residue metalloprotein is presented. The protein binds a variety of metal ions with the appropriate stoichiometry. The diiron protein exhibits catalytic activity with regard to several peroxidase substrates.
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(2003)
J Mol Biol
, vol.334
, pp. 1101-1115
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Calhoun, J.R.1
Kono, H.2
Lahr, S.3
Wang, W.4
Degrado5
Saven, J.G.W.F.6
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55
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0034612192
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Retrostructural analysis of metalloproteins: Application to the design of a minimal model for diiron proteins
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A. Lombardi, C.M. Summa, S. Geremia, L. Randaccio, V. Pavone, and W.F. DeGrado Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins Proc Natl Acad Sci USA 97 2000 6298 6305
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(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 6298-6305
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Lombardi, A.1
Summa, C.M.2
Geremia, S.3
Randaccio, L.4
Pavone5
Degrado, W.F.V.6
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