Secondary structural changes of homologous proteins, lysozyme and α-lactalbumin, in thermal denaturation up to 130 °c and sodium dodecyl sulfate (SDS) effects on these changes: Comparison of thermal stabilities of sds-induced helical structures in these proteins

Langmuir

Volumn 28, Issue 47, 2012, Pages 16268-16273

  Moriyama, Yoshiko ^a   Kondo, Naoaki ^a   Takeda, Kunio ^a  

^a OKAYAMA UNIVERSITY OF SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HELICAL STRUCTURES; HOMOLOGOUS PROTEINS; SODIUM DODECYL SULFATE; STRUCTURAL CHANGE; TEMPERATURE RANGE; THERMAL DENATURATIONS;

ENZYMES; SODIUM; SODIUM SULFATE; THERMODYNAMIC STABILITY;

PROTEINS;

DODECYL SULFATE SODIUM; LACTALBUMIN; LYSOZYME;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; COMPARATIVE STUDY; DRUG EFFECT; ENZYME STABILITY; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; TEMPERATURE;

ANIMALS; CATTLE; ENZYME STABILITY; LACTALBUMIN; MURAMIDASE; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM DODECYL SULFATE; TEMPERATURE;

EID: 84870199479     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la3035598     Document Type: Article

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