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Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly beta-sheet protein.
Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus.
Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment.
Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins.
Finding the fittest fold: using the evolutionary record to design new proteins.
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Finding the fittest fold: using the evolutionary record to design new proteins.
Smock RG, Gierasch LM. Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 2005 Sep 23; 122(6):832-4.
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PubMed
subject areas
Amino Acid Sequence
Amino Acids
Data Interpretation, Statistical
Evolution, Molecular
Molecular Sequence Data
Protein Engineering
Protein Folding
Proteins
authors with profiles
Lila M Gierasch Ph.D.