NMR paper Real-time NMR kinetic studies provide global and residue-specific information on the

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[NMR paper] Real-time NMR kinetic studies provide global and residue-specific information on the

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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

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Amber

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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

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RCI

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HADDOCK

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Poulsen_rc_CS

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11-24-2010, 09:01 PM

nmrlearner

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Real-time NMR kinetic studies provide global and residue-specific information on the

Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.

Related Articles Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.

J Mol Biol. 2003 May 2;328(3):693-703

Authors: Roy M, Jennings PA

The interleukin-1beta (IL-1beta) structural motif is a beta-trefoil super fold created by six two-stranded beta-hairpins. Turns are thus particularly important in creating the topology and the arrangement of beta-strands in this structural motif. In contrast to the signals observed in optical studies, real-time NMR kinetic investigations of the denaturant-induced unfolding of interleukin-1beta provide direct, global, and residue-specific information on the structural nature of the unfolding reaction. Heterogeneity in the individual amino acid residue kinetics reveals a rugged unfolding landscape. The relative kinetic stability of native-like turns supports low temperature molecular dynamics predictions of turn-controlled unfolding.

PMID: 12706726 [PubMed - indexed for MEDLINE]

Source: PubMed

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