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Simplified proteins: minimalist solutions to the 'protein folding problem'.

Author

Kevin W Plaxco

1965 -

David Baker

1962 -

Published in: Current Opinion in Structural Biology

Date of publication: February 1, 1998

Main subject: protein folding

Bibliographic databases:

Cites articles 46

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Design of a "minimAl" homeodomain: the N-terminal arm modulates DNA binding affinity and stabilizes homeodomain structure
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Folded proteins occur frequently in libraries of random amino acid sequences
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Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
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Sequence 'minimization': exploring the sequence landscape with simplified sequences,Sequence ‘minimization’: exploring the sequence landscape with simplified sequences
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De novo design of the hydrophobic cores of proteins
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A phage display system for studying the sequence determinants of protein folding
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Cooperatively folded proteins in random sequence libraries
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Structures of folding intermediates
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Ice-binding structure and mechanism of an antifreeze protein from winter flounder
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Evidence for nonrandom hydrophobicity structures in protein chains
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Protein folding from a combinatorial perspective
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Active barnase variants with completely random hydrophobic cores
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What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
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A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
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Sequence space, folding and protein design

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