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C N Pace

Showing results (41-50 of 65) with videos related to

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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 mutantB A Shirley, P Stanssens, J Steyaert, et al.
Biochemistry|November 17, 1992
Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1I M Plaza del Pino, C N Pace, E Freire
Biochemistry|January 28, 1992
Contribution of hydrogen bonding to the conformational stability of ribonuclease T1B A Shirley, P Stanssens, U Hahn, et al.
Biochemistry|March 22, 1994
Energetics of ribonuclease T1 structureY 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 proteinC 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----AlaM 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 bondsC 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 foldingC 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 T1J 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 intermediateJ K Grimsley, J M Scholtz, C N Pace, et al.
Pageof 7

Showing results (41-50 of 65) with videos related to

Sort By:
Pageof 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 mutantB A Shirley, P Stanssens, J Steyaert, et al.
Biochemistry|November 17, 1992
Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1I M Plaza del Pino, C N Pace, E Freire
Biochemistry|January 28, 1992
Contribution of hydrogen bonding to the conformational stability of ribonuclease T1B A Shirley, P Stanssens, U Hahn, et al.
Biochemistry|March 22, 1994
Energetics of ribonuclease T1 structureY 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 proteinC 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----AlaM 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 bondsC 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 foldingC 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 T1J 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 intermediateJ K Grimsley, J M Scholtz, C N Pace, et al.
Pageof 7