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K Saraboji

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

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Biochemical and Biophysical Research Communications|December 31, 2003
Purification and crystallization of haemoglobin from donkey (Equus asinus)D Balasundaresan, K Saraboji, M N Ponnuswamy
Biochimie|February 21, 2006
Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolutionD Balasundaresan, K Saraboji, M N Ponnuswamy
Indian Journal of Biochemistry & Biophysics|August 21, 2012
A study of aromatic hydrogen bonds of peptides with aromatic amino acid side-chainsA Nallini, K Saraboji, M N Ponnuswamy
Journal of Molecular Graphics & Modelling|January 27, 2016
Contribution of main chain and side chain atoms and their locations to the stability of thermophilic proteinsDharma Rao Tompa, M Michael Gromiha, K Saraboji
Biopolymers|February 3, 2006
Average assignment method for predicting the stability of protein mutantsK Saraboji, M Michael Gromiha, M N Ponnuswamy
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|February 7, 2013
Purification, crystallization and preliminary crystallographic studies of haemoglobin from mongoose (Helogale parvula) in two different crystal forms induced by pH variationM Mohamed Abubakkar, K Saraboji, M N Ponnuswamy
Computational Biology and Chemistry|February 1, 2005
Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymesK Saraboji, M Michael Gromiha, M N Ponnuswamy
International Journal of Biological Macromolecules|April 7, 2005
Importance of main-chain hydrophobic free energy to the stability of thermophilic proteinsK Saraboji, M Michael Gromiha, M N Ponnuswamy
Biophysical Chemistry|November 5, 2005
Role of amino acid properties to determine backbone tau(N-Calpha-C') stretching angle in peptides and proteinsS M Malathy Sony, K Saraboji, N Sukumar, et al.
Biophysical Chemistry|February 18, 2004
Role of non-covalent interactions for determining the folding rate of two-state proteinsM Michael Gromiha, K Saraboji, Shandar Ahmad, et al.
Pageof 2

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

Sort By:
Pageof 2
Biochemical and Biophysical Research Communications|December 31, 2003
Purification and crystallization of haemoglobin from donkey (Equus asinus)D Balasundaresan, K Saraboji, M N Ponnuswamy
Biochimie|February 21, 2006
Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolutionD Balasundaresan, K Saraboji, M N Ponnuswamy
Indian Journal of Biochemistry & Biophysics|August 21, 2012
A study of aromatic hydrogen bonds of peptides with aromatic amino acid side-chainsA Nallini, K Saraboji, M N Ponnuswamy
Journal of Molecular Graphics & Modelling|January 27, 2016
Contribution of main chain and side chain atoms and their locations to the stability of thermophilic proteinsDharma Rao Tompa, M Michael Gromiha, K Saraboji
Biopolymers|February 3, 2006
Average assignment method for predicting the stability of protein mutantsK Saraboji, M Michael Gromiha, M N Ponnuswamy
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|February 7, 2013
Purification, crystallization and preliminary crystallographic studies of haemoglobin from mongoose (Helogale parvula) in two different crystal forms induced by pH variationM Mohamed Abubakkar, K Saraboji, M N Ponnuswamy
Computational Biology and Chemistry|February 1, 2005
Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymesK Saraboji, M Michael Gromiha, M N Ponnuswamy
International Journal of Biological Macromolecules|April 7, 2005
Importance of main-chain hydrophobic free energy to the stability of thermophilic proteinsK Saraboji, M Michael Gromiha, M N Ponnuswamy
Biophysical Chemistry|November 5, 2005
Role of amino acid properties to determine backbone tau(N-Calpha-C') stretching angle in peptides and proteinsS M Malathy Sony, K Saraboji, N Sukumar, et al.
Biophysical Chemistry|February 18, 2004
Role of non-covalent interactions for determining the folding rate of two-state proteinsM Michael Gromiha, K Saraboji, Shandar Ahmad, et al.
Pageof 2