NMR paper 1H resonance assignments, secondary structure and general topology of single-chain mo

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[NMR paper] 1H resonance assignments, secondary structure and general topology of single-chain mo

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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, 11:45 PM

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1H resonance assignments, secondary structure and general topology of single-chain mo

1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR.

Related Articles 1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR.

J Biomol NMR. 1992 Nov;2(6):557-72

Authors: Tomic MT, Somoza JR, Wemmer DE, Park YW, Cho JM, Kim SH

We determined the resonance assignments, secondary structure and general topology of the 11-kDa sweet protein single-chain monellin (SCM), using two-dimensional proton nuclear magnetic resonance spectroscopy (2D-NMR). SCM is a genetically engineered protein whose design is based on the crystal structure of natural, two-chain monellin (Kim et al., 1989). Analysis of the NMR spectra shows that the secondary structure of SCM consists of a five-strand anti-parallel beta-sheet and a 15-residue alpha-helix. Tertiary NOE constraints place the alpha-helix on the hydrophobic side of the beta-sheet, and indicate that the sheet is partially wrapped around the helix. The general structural features determined for SCM are similar to those of native monellin (Ogata et al., 1987). Some differences between the SCM structure in solution and the crystal structure of monellin are discussed.

PMID: 1490107 [PubMed - indexed for MEDLINE]

Source: PubMed

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