Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable

Protein Science

Volumn 11, Issue 1, 2002, Pages 174-177

  Loladze, V V ^a   Makhatadze, G I ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

Balance of forces; Chemical denaturation; Chemical modification; Circular dichroism spectroscopy; Electrostatic interactions; Energetics; Protein stability

Indexed keywords

ARGININE; LYSINE; UBIQUITIN;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; ELECTRICITY; ENERGY TRANSFER; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; SURFACE CHARGE;

CIRCULAR DICHROISM; DOSE-RESPONSE RELATIONSHIP, DRUG; FUNGAL PROTEINS; HYDROGEN-ION CONCENTRATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTONS; THERMODYNAMICS; UBIQUITIN; UREA;

EID: 0036136161     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.29902     Document Type: Article

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