hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment i

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hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment i

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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:

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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Methyl S2

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Shiftx2

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ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

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Solid-state NMR:

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08-16-2010, 03:50 AM

nmrlearner

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hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment i

hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment in (13C, 15N) labeled proteins

Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 30 June 2010

Dinesh, Kumar , Jithender G, Reddy , Ramakrishna V., Hosur

Time-saving in data acquisition is a major thrust of NMR pulse sequence development in the context of structural proteomics research. The conventional HNCA and HN(CA)CO pulse sequences, routinely used for sequential backbone assignment, have the limitation that they cannot distinguish inter- and intra-residue correlations. In order to remove this ambiguity, one has to record HNCO and HN(CO)CA or sequential HNCA experiments which provide unambiguous information of sequential correlations. However, this almost doubles the experimental time. Besides, they require repeated scanning through the 15N planes to search for the matching peaks along the carbon dimension. In this background, we present here...

Source: Journal of Magnetic Resonance

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