NMR paper Solution structure and dynamics of integral membrane proteins by NMR: a case study in

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[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in

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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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11-24-2010, 11:14 PM

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Solution structure and dynamics of integral membrane proteins by NMR: a case study in

Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.

Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.

Methods Enzymol. 2005;394:335-50

Authors: Hwang PM, Kay LE

Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide (15)N-(1)H groups to obtain sequence-specific chemical shift assignments, structural restraints, and a wide range of dynamics information. These methods have proven successful in the study of the outer membrane enzyme, PagP, not only for obtaining the global fold of the protein but also for characterizing in detail the conformational fluctuations that are critical to its activity. NMR methods can also be extended to take advantage of slowly relaxing methyl groups, providing additional probes of structure and dynamics at side chain positions. The current work on PagP demonstrates how solution NMR can provide a unique atomic resolution description of the dynamic processes that are key to the function of many membrane protein systems.

PMID: 15808227 [PubMed - indexed for MEDLINE]

Source: PubMed

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