Sulfate stabilizes the folding intermediate more than the native structure of endostatin

Archives of Biochemistry and Biophysics

Volumn 471, Issue 2, 2008, Pages 232-239

  Fu, Yan ^a   Wu, Xiaoyu ^a   Han, Qing ^a   Liang, Yun ^a   He, Yingbo ^a   Luo, Yongzhang ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

Endostatin; Folding stability; Heparin binding; Protein folding; Sulfate anions

Indexed keywords

ACID; ENDOSTATIN; HEPARIN; SODIUM SULFATE; SULFATE; TRYPTOPHAN; UREA;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE; HEAT TREATMENT; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SENSITIZATION;

ACIDS; ANGIOGENESIS INHIBITORS; ANIONS; CIRCULAR DICHROISM; ENDOSTATINS; HEPARIN; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SULFATES; TEMPERATURE; TIME FACTORS; UREA;

EID: 39849110421     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2007.12.011     Document Type: Article

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