NMR paper The proteolysis process in fermented sausage model systems as studied by nmr relaxometry.

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[NMR paper] The proteolysis process in fermented sausage model systems as studied by nmr relaxometry.

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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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03-10-2015, 07:22 PM

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The proteolysis process in fermented sausage model systems as studied by nmr relaxometry.

THE PROTEOLYSIS PROCESS IN FERMENTED SAUSAGE MODEL SYSTEMS AS STUDIED BY NMR RELAXOMETRY.

Related Articles THE PROTEOLYSIS PROCESS IN FERMENTED SAUSAGE MODEL SYSTEMS AS STUDIED BY NMR RELAXOMETRY.

J Agric Food Chem. 2015 Mar 9;

Authors: Garcia AB, Larsen LB, Cambero MI, Diaz KP, Bertram HC

Abstract
Proton NMR relaxation analyses were performed in sausage model systems (SMS) at different manufacturing times (0, 1, 3, 5, 7 and 9 days) to evaluate changes in water distribution and mobility. Three different water populations were identified: T2b (5-10 ms), T21 (30-70 ms) and T22 (100-300 ms) and the progress of ripening could be followed as a shift towards shorter relaxation times. In addition, the effect of commercial proteases (pronase E and aspartyl proteinase) on protein breakdown and structural integrity of sausage models (SMS+P) was investigated, resulting in the formation of a more fluid and less organized meat matrix that led to the absence of the T22 population until day 9. A very different protein degradation pattern between SMS and SMS+P was obtained by means of electrophoresis SDS-PAGE, supporting that some degree of aggregation is needed for the presence of the T22 population in fermented sausages.

PMID: 25751613 [PubMed - as supplied by publisher]

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