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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.
Evoked Potentials, Motor
The dependability of students' ratings of preceptors.
Intrinsic tryptophans of CRABPI as probes of structure and folding.
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Intrinsic tryptophans of CRABPI as probes of structure and folding.
Clark PL, Liu ZP, Zhang J, Gierasch LM. Intrinsic tryptophans of CRABPI as probes of structure and folding. Protein Sci. 1996 Jun; 5(6):1108-17.
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subject areas
Circular Dichroism
Fluorescence
Gene Expression
Point Mutation
Protein Conformation
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Receptors, Retinoic Acid
Recombinant Proteins
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Titrimetry
Tretinoin
Tryptophan
Urea
authors with profiles
Lila M Gierasch Ph.D.