Fourier-transform infrared spectroscopic investigation of protein stability in the lyophilized form

Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

Volumn 1253, Issue 1, 1995, Pages 69-74

  Costantino, Henry R ^a   Griebenow, Kai ^a   Mishra, Prashant ^a   Langer, Robert ^a   Klibanov, Alexander M ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

FTIR; Lyophilization; Moisture induced aggregation; Protein stability; Recombinant human albumin; Secondary structure

Indexed keywords

HUMAN SERUM ALBUMIN; RECOMBINANT ALBUMIN; UNCLASSIFIED DRUG;

ARTICLE; FOURIER TRANSFORMATION; FREEZE DRYING; INFRARED SPECTROPHOTOMETRY; PRIORITY JOURNAL; PROTEIN STABILITY;

DEXTRANS; FREEZE DRYING; HUMAN; HYDROGEN-ION CONCENTRATION; MURAMIDASE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SERUM ALBUMIN; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; WATER;

EID: 0028875052     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/0167-4838(95)00156-O     Document Type: Article

References (20)

1. Lyophilization-induced reversible changes in the secondary structure of proteins.
2. The hydration of protein secondary structures