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- W1566789051 abstract "This chapter discusses chemical synthesis and nuclear magnetic resonance characterization of partially folded proteins. Partially folded conformations of proteins are commonly induced by extreme solvent conditions such as low pH and addition of alcohol or denaturants. An approach has been developed by which appropriately designed protein analogs, accessible only by chemical synthesis, form partially folded conformations at physiological pH without addition of denaturants or alcohol. As a case study to develop the tools for this general approach, the work has focused on the small 58-residue antiparallel β-sheet protein bovine pancreatic trypsin inhibitor (BPTI). The chapter outlines chemical synthetic methods used to access these molecules, including variants containing stable isotopically labeled residues at strategic positions. . The structures of the resultant BPTI analogs that are either partially folded or completely unfolded are then characterized by two-dimensional IH homonuclear and 15N heteronuclear nuclear magnetic resonance (NMR) methods." @default.
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- W1566789051 date "1997-01-01" @default.
- W1566789051 modified "2023-10-15" @default.
- W1566789051 title "[27] Chemical synthesis and nuclear magnetic resonance characterization of partially folded proteins" @default.
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- W1566789051 doi "https://doi.org/10.1016/s0076-6879(97)89066-0" @default.
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