NMR studies of protein structure and dynamics - A look backwards and forwards.

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NMR studies of protein structure and dynamics - A look backwards and forwards.

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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:

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Methyl S2

B-factor

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Shiftx2

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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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09-03-2011, 06:55 PM

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NMR studies of protein structure and dynamics - A look backwards and forwards.

NMR studies of protein structure and dynamics - A look backwards and forwards.

NMR studies of protein structure and dynamics - A look backwards and forwards.

J Magn Reson. 2011 Aug 30;

Authors: Kay LE

Abstract
NMR spectroscopy has evolved to become one of the most powerful tools for the study of protein structure and dynamics. Advances over the past decade have greatly extended the methodology to studies of molecules of ever increasing complexity. Herein I provide a short perspective relating the circumstances that led to some of the contributions from my laboratory in this area and highlight how these original experiments, summarized in a Journal of Magnetic Resonance article in 2005 (JMR, 173 193-207), have influenced the current focus of my research.

PMID: 21885309 [PubMed - as supplied by publisher]

Source: PubMed

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