NMR paper High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy

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[NMR paper] High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

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08-21-2010, 11:41 PM

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High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy

High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy.

Related Articles High protein mobility in skinned rabbit muscle fibres observed by 1H NMR spectroscopy.

FEBS Lett. 1992 Feb 24;298(2-3):226-8

Authors: Kalbitzer HR, Schrumpf M, Wray J

1H NMR spectra of skinned rabbit muscle fibers show a group of relatively sharp resonance lines which presumably originate from highly mobile protein domains. Comparison with the spectrum of myosin subfragment 1 suggests that these signals may come at least partly from mobile regions of the myosin head. NMR could possibly be used to characterize the movements of crossbridges in force generation.

PMID: 1544450 [PubMed - indexed for MEDLINE]

Source: PubMed

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