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Independent folding and conformational changes of the barnase module in the VL-barnase immunofusion: calorimetric evidence

FEBS Letters

Jan 16, 2004

Yaroslav I TsybovskySergey P Martsev

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Abstract

Although stability is critical for in vivo application of immunotoxins, a thermodynamic description of their folding/stability is still lacking. We applied differential scanning calorimetry (DSC) to RNase-based immunofusion comprising barnase, cytotoxic RNase from Bacillus amyloliquefac...read more

Mentioned in this Paper

Hybrid Proteins, Recombinant
Thermodynamics
Ligands
Bacillus amyloliquefaciens ribonuclease
Pancreatic ribonuclease
Guanosine
Immunotoxins
Protein Folding, Globular
Endoribonucleases
Bacterial Proteins
Paper Details
References
  • References29
  • Citations2
123

Independent folding and conformational changes of the barnase module in the VL-barnase immunofusion: calorimetric evidence

FEBS Letters

Jan 16, 2004

Yaroslav I TsybovskySergey P Martsev

PMID: 14741376

DOI: 10.1016/s0014-5793(03)01509-6

Abstract

Although stability is critical for in vivo application of immunotoxins, a thermodynamic description of their folding/stability is still lacking. We applied differential scanning calorimetry (DSC) to RNase-based immunofusion comprising barnase, cytotoxic RNase from Bacillus amyloliquefac...read more

Mentioned in this Paper

Hybrid Proteins, Recombinant
Thermodynamics
Ligands
Bacillus amyloliquefaciens ribonuclease
Pancreatic ribonuclease

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Paper Details
References
  • References29
  • Citations2
123

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