NMR paper High-resolution 2D 1H-15N NMR characterization of persistent structural alterations o

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[NMR paper] High-resolution 2D 1H-15N NMR characterization of persistent structural alterations o

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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

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RCI

Interactions from chemical shifts:

HADDOCK

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RDCs:

Pseudocontact shifts:

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SAVES2 or SAVES4

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FANDAS

MestReS

V-NMR

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Backbone S2

Methyl S2

B-factor

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Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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MAXOCC

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CCPN

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DisMeta

Protein solubility:

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11-25-2010, 08:21 PM

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High-resolution 2D 1H-15N NMR characterization of persistent structural alterations o

High-resolution 2D 1H-15N NMR characterization of persistent structural alterations of proteins induced by interactions with silica nanoparticles.

Related Articles High-resolution 2D 1H-15N NMR characterization of persistent structural alterations of proteins induced by interactions with silica nanoparticles.

Langmuir. 2005 Jun 21;21(13):5974-9

Authors: Lundqvist M, Sethson I, Jonsson BH

The binding of protein to solid surfaces often induces changes in the structure, and to investigate these matters we have selected two different protein-nanoparticle systems. The first system concerns the enzyme human carbonic anhydrase II which binds essentially irreversibly to the nanoparticles, and the second system concerns human carbonic anhydrase I which alternate between the adsorbed and free state upon interaction with nanoparticles. Application of the TROSY pulse sequence has allowed high-resolution NMR analysis for both of the protein-nanoparticle systems. For HCAII it was possible to observe spectra of protein when bound to the nanoparticles. The results indicated that HCAII undergoes large rearrangements, forming an ensemble of molten globule-like structures on the surface. The spectra from the HCAI-nanoparticle system are dominated by HCAI molecules in solution. A comparative analysis of variations in intensity from 97 amide resonances in a 1H-15N TROSY spectrum revealed the effects from interaction with nanoparticle on the protein structure at amino acid resolution.

PMID: 15952849 [PubMed - indexed for MEDLINE]

Source: PubMed

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