NMR paper Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

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[NMR paper] Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

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NMR processing:

MDD

NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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FANDAS

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Methyl S2

B-factor

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Shiftx2

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ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

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Protein disorder:

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11-17-2010, 11:06 PM

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Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

Related Articles Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.

FEBS Lett. 1998 Feb 13;423(1):110-2

Authors: Killick TR, Freund SM, Fersht AR

The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR. Rate constants for changes in individual residues during the unfolding or refolding of the mutants studied by real-time NMR are all within experimental error of the overall process of folding/unfolding measured by stopped-flow measurements of tryptophan fluorescence. Folding of these mutants is thus highly co-operative. Changes in the tryptophan fluorescence give accurate measurements of the protein folding process.

PMID: 9506851 [PubMed - indexed for MEDLINE]

Source: PubMed

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