NMR paper Motional effects on NMR structural data. Comparison of spinach and Escherichia coli a

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[NMR paper] Motional effects on NMR structural data. Comparison of spinach and Escherichia coli a

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NMR processing:

MDD

NMR assignment:

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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

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HADDOCK

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SAVES2 or SAVES4

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Methyl S2

B-factor

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PPM

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Shifty

Camcoil

Poulsen_rc_CS

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08-21-2010, 10:48 PM

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Motional effects on NMR structural data. Comparison of spinach and Escherichia coli a

Motional effects on NMR structural data. Comparison of spinach and Escherichia coli acyl carrier proteins.

Related Articles Motional effects on NMR structural data. Comparison of spinach and Escherichia coli acyl carrier proteins.

Biochem Pharmacol. 1990 Jul 1;40(1):7-13

Authors: Kim Y, Ohlrogge JB, Prestegard JH

Proteins in solution need not exist in a single rigid structure but can exist in a dynamic equilibrium among structural forms. The problems that this poses for structure determination using nuclear Overhauser effect data from two-dimensional NMR experiments are discussed and illustrated with data on functionally equivalent proteins from two different species. One of these proteins, acyl carrier protein from Escherichia coli, shows a single set of resonances, easily interpreted on the basis of a single rigid structure. However, the related protein, acyl carrier protein from spinach, shows two sets of resonances, suggesting that two conformers in dynamic equilibrium would be a better structural model.

PMID: 2196884 [PubMed - indexed for MEDLINE]

Source: PubMed

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