Amyloid fibril formation by native and modified bovine β- lactoglobulins proceeds through unfolded form of proteins: A comparative study

Biophysical Chemistry

Volumn 159, Issue 2-3, 2011, Pages 311-320

  Ghadami, Seyyed Abolghasem ^a,b   Khodarahmi, Reza ^b,c   Ghobadi, Sirous ^a   Ghasemi, Moosa ^c   Pirmoradi, Saeed ^d  

^a RAZI UNIVERSITY   (Iran)

^b KERMANSHAH UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^c KERMANSHAH UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^d ISLAMIC AZAD UNIVERSITY   (Iran)

Author keywords

Lactoglobulin; Aggregation; Amyloid fibrillation; Chemical modification; Unfolding

Indexed keywords

AMYLOID; BETA LACTOGLOBULIN; LYSINE;

ALGORITHM; ARTICLE; CHEMICAL MODIFICATION; COMPARATIVE STUDY; CONTROLLED STUDY; FLUOROMETRY; KINETICS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN UNFOLDING; THEORETICAL STUDY; THERMODYNAMICS; TURBIDIMETRY;

AMYLOID; ANIMALS; CATTLE; CIRCULAR DICHROISM; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LACTOGLOBULINS; LYSINE; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN UNFOLDING; THERMODYNAMICS;

BOVINAE;

EID: 80053371263     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.08.004     Document Type: Article

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