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P McPhie

Showing results (1-10 of 93) with videos related to

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Biochemistry|December 2, 1975
The origin of the alkaline inactivation of pepsinogenP McPhie
The Journal of Biological Chemistry|May 10, 1980
Kinetic studies on the unfolding and refolding of pepsinogen in urea. The nature of the rate-limiting stepP McPhie
Biophysical Chemistry|May 1, 1975
The alkaline transition of swine pepsinogenP McPhie
Biophysical Chemistry|May 1, 1979
The alkaline transition of swine pepsinogenP McPhie
Analytical Biochemistry|May 25, 2001
Circular dichroism studies on proteins in films and in solution: estimation of secondary structure by g-factor analysisP McPhie
The Journal of Biological Chemistry|July 10, 1977
On the apparent inhibition of intramolecular activation of pepsinogen by pepsin substratesP McPhie
Developments in Biological Standardization|January 16, 1999
Estimation of secondary/tertiary structureP McPhie
Biochemistry|October 26, 1982
Swine pepsinogen folding intermediates are highly structured, motile moleculesP McPhie
Biochemical and Biophysical Research Communications|January 16, 1989
A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanismP McPhie
Biochemistry|January 24, 1978
Thermodynamics of the denaturation of pepsinogen by ureaF Ahmad, P McPhie
Pageof 10

Showing results (1-10 of 93) with videos related to

Sort By:
Pageof 10
Biochemistry|December 2, 1975
The origin of the alkaline inactivation of pepsinogenP McPhie
The Journal of Biological Chemistry|May 10, 1980
Kinetic studies on the unfolding and refolding of pepsinogen in urea. The nature of the rate-limiting stepP McPhie
Biophysical Chemistry|May 1, 1975
The alkaline transition of swine pepsinogenP McPhie
Biophysical Chemistry|May 1, 1979
The alkaline transition of swine pepsinogenP McPhie
Analytical Biochemistry|May 25, 2001
Circular dichroism studies on proteins in films and in solution: estimation of secondary structure by g-factor analysisP McPhie
The Journal of Biological Chemistry|July 10, 1977
On the apparent inhibition of intramolecular activation of pepsinogen by pepsin substratesP McPhie
Developments in Biological Standardization|January 16, 1999
Estimation of secondary/tertiary structureP McPhie
Biochemistry|October 26, 1982
Swine pepsinogen folding intermediates are highly structured, motile moleculesP McPhie
Biochemical and Biophysical Research Communications|January 16, 1989
A reversible unfolding reaction of swine pepsin; implications for pepsinogen's folding mechanismP McPhie
Biochemistry|January 24, 1978
Thermodynamics of the denaturation of pepsinogen by ureaF Ahmad, P McPhie
Pageof 10