Sparsely-sampled High-resolution 4-D Experiments for Efficient Backbone Resonance Assignment of Disordered Proteins

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Sparsely-sampled High-resolution 4-D Experiments for Efficient Backbone Resonance Assignment of Disordered Proteins

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Structure from NMR restraints:

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Torsion angles from chemical shifts:

Preditor

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Secondary structure from chemical shifts:

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TALOS

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ArShift- Aromatic

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Camcoil

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01-05-2011, 11:03 AM

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Sparsely-sampled High-resolution 4-D Experiments for Efficient Backbone Resonance Assignment of Disordered Proteins

Sparsely-sampled High-resolution 4-D Experiments for Efficient Backbone Resonance Assignment of Disordered Proteins

Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 4 January 2011

Jie, Wen , Jihui, Wu , Pei, Zhou

Intrinsically disordered proteins (IDPs) play important roles in many critical cellular processes. Due to their limited chemical shift dispersion, IDPs often require four pairs of resonance connectivities (H?, C?, C? and CO) for establishing sequential backbone assignment. Because most conventional 4-D triple-resonance experiments share an overlapping C? evolution period, combining existing 4-D experiments does not offer an optimal solution for non-redundant collection of a complete set of backbone resonances. Using alternative chemical shift evolution schemes, we propose a new pair of 4-D triple resonance experiments—HA(CA)CO(CA)NH/ HA(CA)CONH—that complement the 4-D HNCACB/ HN(CO)CACB experiments to provide complete backbone resonance information. Collection of...

Source: Journal of Magnetic Resonance

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