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PDBsum entry 1le0
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De novo protein
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PDB id
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1le0
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References listed in PDB file
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Key reference
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Title
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Tryptophan zippers: stable, Monomeric beta -Hairpins.
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Authors
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A.G.Cochran,
N.J.Skelton,
M.A.Starovasnik.
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Ref.
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Proc Natl Acad Sci U S A, 2001,
98,
5578-5583.
[DOI no: ]
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PubMed id
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Abstract
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A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the
beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length)
with four different turn sequences are monomeric and fold cooperatively in
water, as has been observed previously for some hairpin peptides. However, the
folding free energies of the trpzips exceed substantially those of all
previously reported beta-hairpins and even those of some larger designed
proteins. NMR structures of three of the trpzip peptides reveal exceptionally
well-defined beta-hairpin conformations stabilized by cross-strand pairs of
indole rings. The trpzips are the smallest peptides to adopt an unique tertiary
fold without requiring metal binding, unusual amino acids, or disulfide
crosslinks.
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Figure 2.
Fig. 2. Equilibrium ultracentrifugation of trpzips 1-3.
The data shown are for 60 µM peptide samples and a rotor
speed of 40 krpm. Apparent molecular weights obtained from the
slopes (assuming ideal behavior) are shown; calculated formula
weights are 1,608 for trpzips 1 and 2 and 1,648 for trpzip3.
Trpzip1 data are offset vertically (ln absorbance  0.085) for
clarity.
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Figure 5.
Fig. 5. NMR analysis of trpzip4. (A) Overlay of the COSY
fingerprint regions for the wild-type gb1 peptide (red) and
trpzip4 (black); the location of crosspeaks are indicated for
both peptides and are labeled for trpzip4. (B) Ensemble of 20
structures of trpzip 4 compared with the minimized mean
structure of the B1 domain of protein G (Protein Data Bank code
2GB1) (30); backbone atoms of protein residues 46-52 were
superposed on the mean coordinates of the ensemble, yielding a
rmsd of 0.67 Å.
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Secondary reference #1
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Title
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Chemical-Shift-Based methods for structure validation and refinement: application to tryptophan zipper beta-Hairpin peptides
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Authors
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N.J.Skelton,
A.G.Cochran,
M.A.Starovasnik.
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Ref.
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TO BE PUBLISHED ...
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