Molecular confinement influences protein structure and enhances thermal protein stability

Protein Science

Volumn 10, Issue 2, 2001, Pages 250-261

  Eggers, D K ^a   Valentine, J S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Apomyoglobin; Circular dichroism; Hofmeister effect; Macromolecular crowding; Protein folding; Sol gel glass

Indexed keywords

ALCOHOL; ALPHA LACTALBUMIN; APOMYOGLOBIN; BUFFER; LYSOZYME; METMYOGLOBIN; POTASSIUM CHLORIDE; SILICON DIOXIDE; SOLVENT; WATER;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; ENCAPSULATION; IONIC STRENGTH; MACROMOLECULE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; STEREOSPECIFICITY; THERMOSTABILITY;

ANIMALS; APOPROTEINS; CALCIUM; CATTLE; CHICKENS; CIRCULAR DICHROISM; DITHIOTHREITOL; EDETIC ACID; HORSES; HYDROGEN-ION CONCENTRATION; IONS; LACTALBUMIN; METMYOGLOBIN; MURAMIDASE; MYOGLOBIN; POTASSIUM CHLORIDE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SILICON DIOXIDE; TEMPERATURE; ULTRAVIOLET RAYS;

EID: 0035092041     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.36201     Document Type: Article

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