Protein NMR of biologicals: analytical support for development and marketed products

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Protein NMR of biologicals: analytical support for development and marketed products

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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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

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

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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04-29-2020, 04:16 PM

nmrlearner

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Protein NMR of biologicals: analytical support for development and marketed products

Protein NMR of biologicals: analytical support for development and marketed products

Abstract

Application of NMR spectroscopy to derive in-depth characterization of structure and dynamical properties of biomolecules is well established nowadays in many laboratories. Most of these methods rest on the availability of protein labeled with stable isotopes like 13C and 15N. In this report examples are presented on the application of NMR spectroscopic methods to characterize biopharmaceutical proteins in cases no isotope labeled material are available. This is typically found in protein samples used in the development of formulations and production processes. Another important focus of this report is the application of NMR methodology in the field of counterfeit drugs of biologicals and biosimilars. Especially here, NMR does offer relevant structural and quantitative data due to the high versatility of the NMR equipment. An excurse regarding the high medical relevance for a detailed spectroscopic analysis of counterfeits will be presented.

Source: Journal of Biomolecular NMR

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