Anisotropy in Protein NMR

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Anisotropy in Protein NMR

• Anisotropic Rotational Diffusion
• Anisotropic Susceptibility
• Chemical Shift Anisotropy

2
s22
C
O
C
N
H
s33
C
s11
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Chemical Shift Anisotropy
s22
s33
s11
s
s//
Isotropic (s11 s22 s33) / 3 Anisotropic
s// - s
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Chemical Shift Anisotropy
Cross correlation
Dipolar Chemical Shift Anisotropy ( D ) (
C )
Relaxation rates ( D C ) 2 ( D - C ) 2
1/T2 - ?
1/T2 ?
15N
HN b gt
HN a gt
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Bax
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N
N
a7
a8
a6
a4
a2
C
C
a1
a9
a3
a5
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Dd (15N) versus DNH for human Bax
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15N CSA refinement of human Bax
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Hydrogen Bond Distance and Angle Correlation
A 0.019 Å-3 B 0.21 Å-3
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Hydrogen Bond Distance and Angle
CorrelationRefinement of Human Bax
without HBDA with HBDA Energies (kcal
mol-1) overall 298.5 7.2 309.6
6.4 NOE 7.2 1.7 8.0 3.1
dipolar 21.7 3.2 21.8 2.3
dihedral 0.32 0.52 0.21 0.30
HBDA N/A 0. 28 0.16 HBDA RMSD
(Å-3) 0.048 0.011 0.007 0.002
pairwise RMSDs (residues 16-188) (Å)
backbone 1.70 0.30 1.51 0.14 heavy
atom 2.45 0.23 2.24 0.13 number
of NOE violations 4.0 2.1 3.6 1.8 number
of angle violations 1.7 1.6 3.3 1.6
Ramachandran plot analysis residues
in core regions () 76.7 2.1 77.2 2.1
residues in additional allowed regions () 17.9
2.1 17.4 1.9 residues in generously
allowed regions () 4.3 1.8 3.8 1.2
residues in disallowed regions () 1.1
0.6 1.7 0.9