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NMR processing:
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NMR assignment:
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PINE
Side-chains:
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NOEs:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
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Template-based:
GeNMR
I-TASSER
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:
Preditor
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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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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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RefDB
NMR model quality:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
iCing
PSVS
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SAVES2 or SAVES4
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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ArShift- Aromatic
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PPM
CheShift-2- Cα
From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Unread 08-14-2010, 04:19 AM
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Default Assessment of GABARAP self-association by its diffusion properties

Abstract Gamma-aminobutyric acid type A receptor-associated protein (GABARAP) belongs to a family of small ubiquitin-like adaptor proteins implicated in intracellular vesicle trafficking and autophagy. We have used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. Our data suggest the presence of distinct conformational states and provide support for self-association of GABARAP molecules. Assuming a monomerÔ??dimer equilibrium, a temperature-dependent dissociation constant could be derived. Based on a temperature series of 1H15N heteronuclear single quantum coherence nuclear magnetic resonance spectra, we propose residues potentially involved in GABARAP self-interaction. The possible biological significance of these observations is discussed with respect to alternative scenarios of oligomerization.
  • Content Type Journal Article
  • DOI 10.1007/s10858-010-9437-5
  • Authors
    • Victor Pacheco, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 3 52425 J├╝lich Germany
    • Peixiang Ma, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 3 52425 J├╝lich Germany
    • Yvonne Thielmann, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 3 52425 J├╝lich Germany
    • Rudolf Hartmann, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 3 52425 J├╝lich Germany
    • Oliver H. Weiergr├Ąber, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 2 52425 J├╝lich Germany
    • Jeannine Mohrl├╝der, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 3 52425 J├╝lich Germany
    • Dieter Willbold, Forschungszentrum J├╝lich Institut f├╝r Strukturbiologie und Biophysik 3 52425 J├╝lich Germany

Source: Journal of Biomolecular NMR
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