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The Journal of Biological Chemistry
|
July 15, 1989
Conformational stability and activity of ribonuclease T1 and mutants. Gln25----Lys, Glu58----Ala, and the double mutant
B A Shirley, P Stanssens, J Steyaert, et al.
Biochemistry
|
November 17, 1992
Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1
I M Plaza del Pino, C N Pace, E Freire
Biochemistry
|
January 28, 1992
Contribution of hydrogen bonding to the conformational stability of ribonuclease T1
B A Shirley, P Stanssens, U Hahn, et al.
Biochemistry
|
March 22, 1994
Energetics of ribonuclease T1 structure
Y Yu, G I Makhatadze, C N Pace, et al.
Protein Science : a Publication of the Protein Society
|
November 1, 1995
How to measure and predict the molar absorption coefficient of a protein
C N Pace, F Vajdos, L Fee, et al.
Biochemistry
|
August 21, 1990
Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala
M McNutt, L S Mullins, F M Raushel, et al.
The Journal of Biological Chemistry
|
August 25, 1988
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
C N Pace, G R Grimsley, J A Thomson, et al.
Protein Science : a Publication of the Protein Society
|
July 28, 1999
Heat capacity change for ribonuclease A folding
C N Pace, G R Grimsley, S T Thomas, et al.
The Journal of Biological Chemistry
|
July 15, 1989
Conformational stability and mechanism of folding of ribonuclease T1
J A Thomson, B A Shirley, G R Grimsley, et al.
Biochemistry
|
December 16, 1997
Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
J K Grimsley, J M Scholtz, C N Pace, et al.
Page
of 7
Search research articles
Search
Showing results (41-50 of 65) with videos related to
Sort By:
Page
of 7
The Journal of Biological Chemistry
|
July 15, 1989
Conformational stability and activity of ribonuclease T1 and mutants. Gln25----Lys, Glu58----Ala, and the double mutant
B A Shirley, P Stanssens, J Steyaert, et al.
Biochemistry
|
November 17, 1992
Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1
I M Plaza del Pino, C N Pace, E Freire
Biochemistry
|
January 28, 1992
Contribution of hydrogen bonding to the conformational stability of ribonuclease T1
B A Shirley, P Stanssens, U Hahn, et al.
Biochemistry
|
March 22, 1994
Energetics of ribonuclease T1 structure
Y Yu, G I Makhatadze, C N Pace, et al.
Protein Science : a Publication of the Protein Society
|
November 1, 1995
How to measure and predict the molar absorption coefficient of a protein
C N Pace, F Vajdos, L Fee, et al.
Biochemistry
|
August 21, 1990
Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala
M McNutt, L S Mullins, F M Raushel, et al.
The Journal of Biological Chemistry
|
August 25, 1988
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
C N Pace, G R Grimsley, J A Thomson, et al.
Protein Science : a Publication of the Protein Society
|
July 28, 1999
Heat capacity change for ribonuclease A folding
C N Pace, G R Grimsley, S T Thomas, et al.
The Journal of Biological Chemistry
|
July 15, 1989
Conformational stability and mechanism of folding of ribonuclease T1
J A Thomson, B A Shirley, G R Grimsley, et al.
Biochemistry
|
December 16, 1997
Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
J K Grimsley, J M Scholtz, C N Pace, et al.
Page
of 7