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NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Default Structure of a compact peptide from staphylococcal nuclease determined by circular di

Structure of a compact peptide from staphylococcal nuclease determined by circular dichroism and NMR spectroscopy.

Related Articles Structure of a compact peptide from staphylococcal nuclease determined by circular dichroism and NMR spectroscopy.

Biochemistry. 1995 May 2;34(17):5795-800

Authors: Maciejewski MW, Zehfus MH

Compact regions in proteins are thought to correspond to domains. If this is true, the structure of a compact region excised from a protein should closely resemble the structure in the intact protein. To test this theory, a compact peptide corresponding to residues 129-142 of staphylococcal nuclease (Ac-EAQAKKEKLNIWS-NH2) was synthesized and its solution structure determined using circular dichroism (CD) and 2D NMR. In aqueous solution, the peptide exhibits CD spectra characteristic of a nascent helix. This nascent helical structure is stabilized by the addition of 2,2,2-trifluoroethanol. Under these conditions, the chemical shift indexes of the 1H alpha and 13C alpha resonances, temperature coefficients of amide protons, and NOE constraints are all consistent with the peptide's structure being a helix-turn. This structure is almost identical to that found in the intact protein.

PMID: 7727439 [PubMed - indexed for MEDLINE]



Source: PubMed
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