Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein

Proteins: Structure, Function and Genetics

Volumn 71, Issue 1, 2008, Pages 35-44

  Stepanenko, Olesya V ^a   Marabotti, Anna ^b   Kuznetsova, Irina M ^a   Turoverov, Konstantin K ^a   Fini, Carlo ^c   Varriale, Antonio ^c,d   Staiano, Maria ^d   Rossi, Mose' ^d   D'Auria, Sabato ^d  

^a INSTITUTE OF CYTOLOGY   (Russian Federation)

^b CNR   (Italy)

^c UNIVERSITY OF PERUGIA   (Italy)

^d INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Circular dichroism; Explosive detection; Fluorescence; Molecular dynamic simulations; Proteins; Thermal denaturation

Indexed keywords

AMINO ACID; BINDING PROTEIN; ODORANT BINDING PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG; WATER;

ANIMAL TISSUE; ARTICLE; EXCITATION; HEAT TREATMENT; HIGH TEMPERATURE; HYDROPHOBICITY; MICROENVIRONMENT; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTUM YIELD; SIMULATION; SPECTROFLUOROMETRY; STRUCTURE ANALYSIS; SWINE; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

SUS;

EID: 40549111967     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21658     Document Type: Article

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