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NMR processing:
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Side-chains:
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NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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iCing
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SAVES2 or SAVES4
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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From structure:
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default Nature of lysozyme-water interactions by proton NMR.

Nature of lysozyme-water interactions by proton NMR.

Related Articles Nature of lysozyme-water interactions by proton NMR.

Biochem Cell Biol. 1991 May-Jun;69(5-6):341-5

Authors: Prosser S, Peemoeller H

Proton spin-lattice relaxation measurements were performed in 10 mM lysozyme solution as a function of temperature and degree of substitution of solvent H2O with D2O. The results show that in the temperature range from 274 to 323 K, the intermolecular lysozyme proton water proton coupling contributes appreciably to the observed water proton relaxation rate. In this system exchange between water protons and labile protein protons does not dominate the behaviour with temperature of the water-lysozyme intermolecular contribution to the spin-lattice relaxation.

PMID: 1654941 [PubMed - indexed for MEDLINE]



Source: PubMed
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