NMR paper NMR relaxation data of water proton in normal tissues.

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[NMR paper] NMR relaxation data of water proton in normal tissues.

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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

Refinement:

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

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

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NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

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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

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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08-22-2010, 02:27 PM

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NMR relaxation data of water proton in normal tissues.

NMR relaxation data of water proton in normal tissues.

Related Articles NMR relaxation data of water proton in normal tissues.

Physiol Chem Phys Med NMR. 1996;28(4):205-38

Authors: Akber SF

The spin lattice relaxation time (T1) and spin spin relaxation time (T2) of water protons of normal human and animal tissues are archived to up-date those already published. The mechanisms for water proton relaxation times of tissues are reviewed with reference to water content, paramagnetic ion, protein dynamics content and organ weight.

PMID: 9153797 [PubMed - indexed for MEDLINE]

Source: PubMed

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