Temperature-jump NMR study of protein folding: Ribonuclease A at low pH

1991 ◽  
Vol 1 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Kazuyuki Akasaka ◽  
Akira Naito ◽  
Hiroshi Nakatani
1988 ◽  
Vol 121 ◽  
Author(s):  
Larry W. Kelts ◽  
Nancy J. Armstrong

ABSTRACTHigh field Silicon-29 NMR is used to study the structural intermediates in tetramethyl and tetraethyl orthosilicate (TMOS and TEOS) low pH sol-gel reactions. Linear oligomers as well as ring components of various sizes are identified and their evolution in the sols is followed. Differences in the number of compact ring structures are related to differences in gel times. Reactions are followed for various silicon alkoxide:water:acid molar ratios.


2005 ◽  
Vol 76 (8) ◽  
pp. 083120 ◽  
Author(s):  
Eefei Chen ◽  
Youxian Wen ◽  
James W. Lewis ◽  
Robert A. Goldbeck ◽  
David S. Kliger ◽  
...  

RSC Advances ◽  
2019 ◽  
Vol 9 (6) ◽  
pp. 3416-3428 ◽  
Author(s):  
Olga A. Francisco ◽  
Courtney J. Clark ◽  
Hayden M. Glor ◽  
Mazdak Khajehpour

Soft anions promote protein folding through binding backbone CH and CH2 groups.


FEBS Letters ◽  
1987 ◽  
Vol 225 (1-2) ◽  
pp. 183-187 ◽  
Author(s):  
Christopher M. Dobson ◽  
Lu-Yun Lian

Biochemistry ◽  
1990 ◽  
Vol 29 (29) ◽  
pp. 6873-6883 ◽  
Author(s):  
Huub J. M. De Groot ◽  
Steven O. Smith ◽  
Jacques Courtin ◽  
Ellen Van den Berg ◽  
Chris Winkel ◽  
...  
Keyword(s):  
Low Ph ◽  

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