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PDBsum entry 2vfo
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References listed in PDB file
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Key reference
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Title
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Side-Chain stacking and beta-Helix stability in p22 tailspike protein
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Authors
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M.Becker,
J.J.Mueller,
T.Weikl,
U.Heinemann,
R.Seckler.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Plasticity and steric strain in a parallel beta-Helix: rational mutations in the p22 tailspike protein.
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Authors
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B.Schuler,
F.Fürst,
F.Osterroth,
S.Steinbacher,
R.Huber,
R.Seckler.
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Ref.
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Proteins, 2000,
39,
89.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. Stereo ribbon drawing of one subunit of the trimeric
TSP  N
prepared with MOLMOL.[59] The domain formed by the large
right-handed  -helix
is in dark grey. Thirteen complete turns wind around the helix
axis and form a long binding groove for the lipopolysaccharide
receptor of phage P22 present on the surface of its host
Salmonella. Bound octasaccharide, a product of the hydrolysis
catalysed by the endorhamnosidase, is indicated by thick lines.
The mutation sites addressed here are indicated as light
spheres. The N-terminus is located in the lower left.
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Figure 4.
Figure 4. Thermal unfolding kinetics in the presence of SDS at
69°C (a), 73°C (b), and 71°C (c), respectively. At
the times indicated, the reactions were stopped by rapid cooling
and analyzed by SDS gel electrophoresis followed by
densitometry. The fraction of monomer band intensity -
corresponding to denatured protein - is plotted against time.
TSP N
wt was included in each experiment for comparison.
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The above figures are
reproduced from the cited reference
with permission from John Wiley & Sons, Inc.
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