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N S Sampson

Showing results (11-20 of 25) with videos related to

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Biochemistry|September 15, 1992
Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomeraseN S Sampson, J R Knowles
Biochemical and Biophysical Research Communications|January 17, 1995
The isomerization catalyzed by Brevibacterium sterolicum cholesterol oxidase proceeds stereospecifically with one baseI J Kass, N S Sampson
Bioorganic & Medicinal Chemistry Letters|January 5, 1999
The importance of GLU361 position in the reaction catalyzed by cholesterol oxidaseI J Kass, N S Sampson
Journal of Molecular Biology|April 5, 2001
The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomeraseJ Xiang, J Sun, N S Sampson
Bioorganic & Medicinal Chemistry|May 20, 2000
Characterization of fertilin beta-disintegrin binding specificity in sperm-egg adhesionS Gupta, H Li, N S Sampson
Biochemistry|May 20, 1997
Investigation of membrane disruption in the reaction catalyzed by cholesterol oxidaseK B Ghoshroy, W Zhu, N S Sampson
Biochemistry|November 7, 2000
Use of the parallax-quench method to determine the position of the active-site loop of cholesterol oxidase in lipid bilayersX Chen, D E Wolfgang, N S Sampson
Proceedings of the National Academy of Sciences of the United States of America|November 1, 2001
Surface molecular recognitionN S Sampson, M Mrksich, C R Bertozzi
Biochemistry|May 16, 1998
Assessment of the role of an omega loop of cholesterol oxidase: a truncated loop mutant has altered substrate specificityN S Sampson, I J Kass, K B Ghoshroy
Biochemistry|November 14, 2001
The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidaseY Yin, N S Sampson, A Vrielink, et al.
Pageof 3

Showing results (11-20 of 25) with videos related to

Sort By:
Pageof 3
Biochemistry|September 15, 1992
Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomeraseN S Sampson, J R Knowles
Biochemical and Biophysical Research Communications|January 17, 1995
The isomerization catalyzed by Brevibacterium sterolicum cholesterol oxidase proceeds stereospecifically with one baseI J Kass, N S Sampson
Bioorganic & Medicinal Chemistry Letters|January 5, 1999
The importance of GLU361 position in the reaction catalyzed by cholesterol oxidaseI J Kass, N S Sampson
Journal of Molecular Biology|April 5, 2001
The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomeraseJ Xiang, J Sun, N S Sampson
Bioorganic & Medicinal Chemistry|May 20, 2000
Characterization of fertilin beta-disintegrin binding specificity in sperm-egg adhesionS Gupta, H Li, N S Sampson
Biochemistry|May 20, 1997
Investigation of membrane disruption in the reaction catalyzed by cholesterol oxidaseK B Ghoshroy, W Zhu, N S Sampson
Biochemistry|November 7, 2000
Use of the parallax-quench method to determine the position of the active-site loop of cholesterol oxidase in lipid bilayersX Chen, D E Wolfgang, N S Sampson
Proceedings of the National Academy of Sciences of the United States of America|November 1, 2001
Surface molecular recognitionN S Sampson, M Mrksich, C R Bertozzi
Biochemistry|May 16, 1998
Assessment of the role of an omega loop of cholesterol oxidase: a truncated loop mutant has altered substrate specificityN S Sampson, I J Kass, K B Ghoshroy
Biochemistry|November 14, 2001
The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidaseY Yin, N S Sampson, A Vrielink, et al.
Pageof 3