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Side-chains:
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Ab initio:
GeNMR
Cyana
XPLOR-NIH
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Fragment-based:
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GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
CSI (via RCI server)
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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Molecular dynamics:
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From structure:
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ArShift- Aromatic
ShiftS
Proshift
PPM
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From sequence:
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Camcoil
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Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
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camGroEL
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Isotope labeling:
UPLABEL
Solid-state NMR:
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Old 08-21-2010, 04:03 PM
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Default Supercontracted spider dragline silk: a solid-state NMR study of the local structure.

Supercontracted spider dragline silk: a solid-state NMR study of the local structure.

Related Articles Supercontracted spider dragline silk: a solid-state NMR study of the local structure.

Int J Biol Macromol. 1999 Mar-Apr;24(2-3):173-8

Authors: van Beek JD, Kümmerlen J, Vollrath F, Meier BH

The local structure of supercontracted dragline silk from the spider Nephila madagascariensis was investigated by solid-state nuclear magnetic resonance. Two-dimensional (2D) spin-diffusion experiments did not show any significant conformational changes in short-range order (and the secondary structure of the protein) upon supercontraction. Our results are in accordance with the proposal by Vollrath et al. (Proc R Soc London B 1996;263:147-151) that urea-supercontraction does not alter the local structure of spider dragline silk fundamentally. However, significant differences in the dynamics of the polypeptide chain upon supercontraction are detected at room temperature. At low temperature, these dynamics are frozen out. In addition, the role of the solvent (water) in the silk is investigated in Nephila edulis. Mobile water is detected at temperatures significantly below the freezing point of bulk water.

PMID: 10342762 [PubMed - indexed for MEDLINE]



Source: PubMed
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