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Fanconi Anemia Complementation Group G Protein
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.
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Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins.
Rotondi KS, Gierasch LM. Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers. 2006; 84(1):13-22.
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PubMed
subject areas
Complementarity Determining Regions
Models, Theoretical
Molecular Chaperones
Molecular Structure
Protein Conformation
Protein Structure, Secondary
Silk
authors with profiles
Lila M Gierasch Ph.D.