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Native structural propensity in cellular retinoic acid-binding protein I 64-88: the role of locally encoded structure in the folding of a beta-barrel protein.
Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A.
The folate pathway is a target for resistance to the drug para-aminosalicylic acid (PAS) in mycobacteria.
Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate.
Probing the folding pathway of a beta-clam protein with single-tryptophan constructs.
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Probing the folding pathway of a beta-clam protein with single-tryptophan constructs.
Clark PL, Weston BF, Gierasch LM. Probing the folding pathway of a beta-clam protein with single-tryptophan constructs. Fold Des. 1998; 3(5):401-12.
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PubMed
subject areas
Circular Dichroism
Fluorescence
Kinetics
Molecular Probes
Protein Structure, Secondary
Receptors, Retinoic Acid
Tryptophan
authors with profiles
Lila M Gierasch Ph.D.