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A R Dinner

Showing results (1-10 of 13) with videos related to

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Nature Structural Biology|March 21, 1998
A metastable state in folding simulations of a protein modelA R Dinner, M Karplus
Journal of Molecular Biology|September 24, 1999
Is protein unfolding the reverse of protein folding? A lattice simulation analysisA R Dinner, M Karplus
Nature Structural Biology|January 3, 2001
The roles of stability and contact order in determining protein folding ratesA R Dinner, M Karplus
Proceedings of the National Academy of Sciences of the United States of America|August 4, 1999
Understanding beta-hairpin formationA R Dinner, T Lazaridis, M Karplus
Protein Engineering|December 10, 1999
Use of a quantitative structure-property relationship to design larger model proteins that fold rapidlyA R Dinner, E Verosub, M Karplus
Proceedings of the National Academy of Sciences of the United States of America|August 6, 1996
The folding mechanism of larger model proteins: role of native structureA R Dinner, A Sali, M Karplus
Proteins|October 21, 1998
Use of quantitative structure-property relationships to predict the folding ability of model proteinsA R Dinner, S S So, M Karplus
IET Systems Biology|November 16, 2010
Defining cooperativity in gene regulation locally through intrinsic noiseM Maienschein-Cline, A Warmflash, A R Dinner
Nature|October 19, 2001
Uracil-DNA glycosylase acts by substrate autocatalysisA R Dinner, G M Blackburn, M Karplus
Proteins|March 25, 1999
Factors that affect the folding ability of proteinsA R Dinner, V Abkevich, E Shakhnovich, et al.
Pageof 2

Showing results (1-10 of 13) with videos related to

Sort By:
Pageof 2
Nature Structural Biology|March 21, 1998
A metastable state in folding simulations of a protein modelA R Dinner, M Karplus
Journal of Molecular Biology|September 24, 1999
Is protein unfolding the reverse of protein folding? A lattice simulation analysisA R Dinner, M Karplus
Nature Structural Biology|January 3, 2001
The roles of stability and contact order in determining protein folding ratesA R Dinner, M Karplus
Proceedings of the National Academy of Sciences of the United States of America|August 4, 1999
Understanding beta-hairpin formationA R Dinner, T Lazaridis, M Karplus
Protein Engineering|December 10, 1999
Use of a quantitative structure-property relationship to design larger model proteins that fold rapidlyA R Dinner, E Verosub, M Karplus
Proceedings of the National Academy of Sciences of the United States of America|August 6, 1996
The folding mechanism of larger model proteins: role of native structureA R Dinner, A Sali, M Karplus
Proteins|October 21, 1998
Use of quantitative structure-property relationships to predict the folding ability of model proteinsA R Dinner, S S So, M Karplus
IET Systems Biology|November 16, 2010
Defining cooperativity in gene regulation locally through intrinsic noiseM Maienschein-Cline, A Warmflash, A R Dinner
Nature|October 19, 2001
Uracil-DNA glycosylase acts by substrate autocatalysisA R Dinner, G M Blackburn, M Karplus
Proteins|March 25, 1999
Factors that affect the folding ability of proteinsA R Dinner, V Abkevich, E Shakhnovich, et al.
Pageof 2