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NMR processing:
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NMR assignment:
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MARS
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PINE
Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
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Template-based:
GeNMR
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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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:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
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RPF scores
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Chemical shifts:
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Vasco
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RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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PSVS
MolProbity
SAVES2 or SAVES4
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Verify_3D
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Old 12-06-2014, 05:18 PM
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Default Recrystallized S-layer protein of a probiotic propionibacterium: structural and nanomechanical changes upon temperature or pH shifts probed by solid-state NMR and AFM.

Recrystallized S-layer protein of a probiotic propionibacterium: structural and nanomechanical changes upon temperature or pH shifts probed by solid-state NMR and AFM.

Recrystallized S-layer protein of a probiotic propionibacterium: structural and nanomechanical changes upon temperature or pH shifts probed by solid-state NMR and AFM.

Langmuir. 2014 Dec 5;

Authors: De Sa Peixoto P, Roiland C, Thomas D, Briard-Bion V, Le Guellec R, Parayre S, Deutsch SM, Jan G, Guyomarc'h F

Abstract
Surface protein layers (S layers) are common constituents of the bacterial cell wall and originate from the assembly of strain-dependent surface layer proteins (Slps). These proteins are thought to play important roles in the bacteria's biology and to have very promising technological applications as biomaterials or as part of cell-host cross-talk in probiotic mechanism. The SlpA from Propionibacterium freudenreichii PFCIRM 118 strain was isolated and recrystallized to investigate organization and assembly of the protein using atomic force microscopy and solid-state 1H and 13C-nuclear magnetic resonance. SlpA was found to form hexagonal p1 monolayer lattices where the protein exhibited high proportions of disordered regions and of bound water. The lattice structure was maintained, but softened, upon mild heating or acidification, probably in relation with the increasing mobilities of the disordered protein regions. These results gave structural insights on the mobile protein regions exposed by S layer films, upon physiologically relevant changes of their environmental conditions.


PMID: 25479375 [PubMed - as supplied by publisher]



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