Natively unfolded human prothymosin α adopts partially folded collapsed conformation at acidic pH

Biochemistry

Volumn 38, Issue 45, 1999, Pages 15009-15016

  Uversky, Vladimir N ^a,b,c   Gillespie, Joel R ^c   Millett, Ian S ^d   Khodyakova, Anna V ^b   Vasiliev, Anatoly M ^b   Chernovskaya, Tatyana V ^b   Vasilenko, Raisa N ^b   Kozlovskaya, Galina D ^b   Dolgikh, Dmitry A ^e   Fink, Anthony L ^c   Doniach, Sebastian ^d   Abramov, Vyacheslav M ^b  

^a INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

^b Institute of Immunology   (Russian Federation)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d STANFORD UNIVERSITY   (United States)

^e SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; PROTHYMOSIN ALPHA; RECOMBINANT PROTEIN; UREA;

ACIDITY; ALPHA HELIX; ANALYTIC METHOD; ARTICLE; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HYDROPHOBICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; SURFACE CHARGE;

CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HUMANS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PRECURSORS; RECOMBINANT PROTEINS; SOLUTIONS; THYMOSIN;

EID: 0033539662     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990752+     Document Type: Article

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