Improvement in protein HSQC spectra from addition of betaine

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Improvement in protein HSQC spectra from addition of betaine

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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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03-10-2025, 09:32 AM

nmrlearner

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Improvement in protein HSQC spectra from addition of betaine

Improvement in protein HSQC spectra from addition of betaine

Addition of glycine betaine up to 1 M gave rise to increased intensity for some weak signals in the HSQC spectra of barnase and Plasmodium falciparum flap endonuclease. The signals that were enhanced were low intensity signals, often from amide groups with rapid internal motion (low order parameter). The majority of signals are however somewhat weaker because of the increased viscosity. Addition of betaine is shown to cause a small but significant overall increase in order parameter, no consistent effect on conformational change on the Âµs-ms timescale, and a reduction in amide exchange rates, by a factor of about 3. The results are consistent with a model in which betaine leads to a reduction in fluctuations within the bulk water, which in turn produces a reduction in internal fluctuations of the protein.

Source: Journal of Biomolecular NMR

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