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本文引用的文献
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Comparison of the folding mechanism of highly homologous proteins in the lipid-binding protein family.
Proteins. 2009 Jun;75(4):799-806. doi: 10.1002/prot.22286.
2
Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR.
Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):11993-8. doi: 10.1073/pnas.0705253104. Epub 2007 Jul 5.
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Coupling ligand recognition to protein folding in an engineered variant of rabbit ileal lipid binding protein.
Chem Commun (Camb). 2006 Nov 28(44):4623-5. doi: 10.1039/b610130e. Epub 2006 Sep 27.
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A residual structure in unfolded intestinal fatty acid binding protein consists of amino acids that are neighbors in the native state.
Biochemistry. 2006 Feb 28;45(8):2608-17. doi: 10.1021/bi052091o.
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Phenylalanine side chain behavior of the intestinal fatty acid-binding protein: the effect of urea on backbone and side chain stability.
J Biol Chem. 2005 Nov 18;280(46):38556-61. doi: 10.1074/jbc.M505435200. Epub 2005 Sep 14.
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The role of Trp-82 in the folding of intestinal fatty acid binding protein.
Proteins. 2005 Oct 1;61(1):176-83. doi: 10.1002/prot.20463.
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Swapping core residues in homologous proteins swaps folding mechanism.
Biochemistry. 2005 Mar 1;44(8):3082-90. doi: 10.1021/bi048125u.
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NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
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The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
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The preparation of 19F-labeled proteins for NMR studies.
Methods Enzymol. 2004;380:400-15. doi: 10.1016/S0076-6879(04)80018-1.
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