scholarly journals Folding Pathway ofEscherichia coliRibonuclease HI:  A Circular Dichroism, Fluorescence, and NMR Study

Biochemistry ◽  
1996 ◽  
Vol 35 (13) ◽  
pp. 4250-4250
Author(s):  
Kazuhiko Yamasaki ◽  
Kyoko Ogasahara ◽  
Katsuhide Yutani ◽  
Motohisa Oobatake ◽  
Shigenori Kanaya
Biochemistry ◽  
1995 ◽  
Vol 34 (51) ◽  
pp. 16552-16562 ◽  
Author(s):  
Kazuhiko Yamasaki ◽  
Kyoko Ogasahara ◽  
Katsuhide Yutani ◽  
Motohisa Oobatake ◽  
Shigenori Kanaya

2012 ◽  
Vol 36 (10) ◽  
pp. 2070 ◽  
Author(s):  
Alexander Prikhod'ko ◽  
Fabrice Pointillart ◽  
Stéphane Golhen ◽  
Konstantin S. Gavrilenko ◽  
Lahcène Ouahab ◽  
...  

2001 ◽  
Vol 2 (3) ◽  
pp. 958-964 ◽  
Author(s):  
Vittorio Crescenzi ◽  
Mariella Dentini ◽  
Maria Scala Bernalda ◽  
Giancarlo Masci ◽  
Vania Rori

Author(s):  
John P. Robinson ◽  
J. David Puett

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.


1968 ◽  
Vol 65 ◽  
pp. 146-151 ◽  
Author(s):  
G. Scheibe ◽  
O. Wörz ◽  
F. Haimerl ◽  
W. Seiffert ◽  
J. Winkler

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