Gamma radiation effects on α-lactalbumin: Structural modifications

Canadian Journal of Physiology and Pharmacology

Volumn 79, Issue 2, 2001, Pages 154-157

  Chapelier, A ^a   Desmadril, M ^a   Houee Levin C ^a  

^a UNIVERSITÉ PARIS SUD   (France)

Author keywords

Ionizing radiation; Protein structural modifications; Protein thermodynamic properties; Radiation induced conformational changes

Indexed keywords

ALPHA LACTALBUMIN; AROMATIC AMINO ACID;

CIRCULAR DICHROISM; CONFERENCE PAPER; GAMMA RADIATION; GEL PERMEATION CHROMATOGRAPHY; MICROCALORIMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE; THERMODYNAMICS;

EID: 0035104737     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y00-075     Document Type: Conference Paper

References (10)

1. Crystal structure of human α-lactalbumin at 1.7 A resolution
2. Protein γ-radiolysis in frozen solutions is a macromolecular surface phenomenon: Fragmentation of lysozyme, citrate synthase and α-lactalbumin in native or denaturated states
3. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
4. Radiolytic protein surface mapping
5. Damage to proteins due to the direct action of ionizing radiation
6. Fluorescence studies of the molecular conformation of α-lactalbumin
7. Radiation effects on the native structure of proteins: Fragmentation without dissociation
8. Circular dichroism spectra of α-lactalbumin
9. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
10. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: Circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor