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NMR processing:
MDD
NMR assignment:
Backbone:
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MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 11-17-2010, 11:15 PM
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Default 1H NMR Self-Diffusion in Polymer-Surfactant Nanocapsules and Cryogels with Enzyme.

1H NMR Self-Diffusion in Polymer-Surfactant Nanocapsules and Cryogels with Enzyme.

Related Articles 1H NMR Self-Diffusion in Polymer-Surfactant Nanocapsules and Cryogels with Enzyme.

J Colloid Interface Sci. 1998 Oct 1;206(1):168-176

Authors: Shapiro YE, Pykhteeva EG, Levashov AV

The multicomponent self-diffusion in nanocapsules and cryogel biocatalytic systems containing alpha-chymotrypsin has been studied with the NMR-PGSE method at various temperatures and compared with the diffusion of such systems without enzyme. Unilamellar vesicles have been formed in water after "coating" with Brij-97 of the poly-(N,N-diallyl-N,N-didodecyl ammonium bromide), poly-DDAB, nanocapsules. The latter have been obtained by UV-irradiation of reversed hydrated micelles from DDAB in cyclohexane. Cryogels were made from poly(vinyl alcohol), PVA, aqueous solutions by a freezing-thawing cyclic process. Both compartmented systems were used as vehicles of the enzyme entrapped in inner aqueous cavities. The activation energies of self-diffusion for both these systems have been calculated. These data contain information concerning morphology and molecular packing. Encapsulation of alpha-chymotrypsin in the poly-DDAB/Brij-97 vesicles and the PVA cryogel lowers the Ds values for all molecules and shifts the cloud point toward the lower temperature. On the contrary, the syneresis point for the PVA cryogel is shifted for 8 degrees toward the higher temperature by the entrapment of the enzyme. Besides, entrapment of alpha-chymotrypsin in the cryogel promotes the increase of the Ea values for the PVA chain on 1.5 kJ/mol below the syneresis point. Such a difference indicates the influence of the H-bond system of PVA hydroxyl groups and water molecules on the interference of the protein globule. Entrapment of alpha-chymotrypsin leads to consolidation of this H-bond system. Copyright 1998 Academic Press.

PMID: 9761640 [PubMed - as supplied by publisher]



Source: PubMed
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