Protein design: From the aspect of water solubility and stability
Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …
sequence and 3D-conformation. Their manipulation represents important aspects of the …
[HTML][HTML] Inter-residue interactions in protein folding and stability
MM Gromiha, S Selvaraj - Progress in biophysics and molecular biology, 2004 - Elsevier
During the process of protein folding, the amino acid residues along the polypeptide chain
interact with each other in a cooperative manner to form the stable native structure. The …
interact with each other in a cooperative manner to form the stable native structure. The …
ProThermDB: thermodynamic database for proteins and mutants revisited after 15 years
ProThermDB is an updated version of the thermodynamic database for proteins and mutants
(ProTherm), which has∼ 31 500 data on protein stability, an increase of 84% from the …
(ProTherm), which has∼ 31 500 data on protein stability, an increase of 84% from the …
Short protocols in molecular biology
Course Description The course enables students to gain basic skills in molecular diagnosis
and karyotyping. This includes: DNA isolation and measurements, electrophoresis of nucleic …
and karyotyping. This includes: DNA isolation and measurements, electrophoresis of nucleic …
Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations
R Guerois, JE Nielsen, L Serrano - Journal of molecular biology, 2002 - Elsevier
We have developed a computer algorithm, FOLDEF (for FOLD-X energy function), to provide
a fast and quantitative estimation of the importance of the interactions contributing to the …
a fast and quantitative estimation of the importance of the interactions contributing to the …
CUPSAT: prediction of protein stability upon point mutations
V Parthiban, MM Gromiha… - Nucleic acids research, 2006 - academic.oup.com
Abstract CUPSAT (Cologne University Protein Stability Analysis Tool) is a web tool to
analyse and predict protein stability changes upon point mutations (single amino acid …
analyse and predict protein stability changes upon point mutations (single amino acid …
ProTherm and ProNIT: thermodynamic databases for proteins and protein–nucleic acid interactions
MDS Kumar, KA Bava, MM Gromiha… - Nucleic acids …, 2006 - academic.oup.com
ProTherm and ProNIT are two thermodynamic databases that contain experimentally
determined thermodynamic parameters of protein stability and protein–nucleic acid …
determined thermodynamic parameters of protein stability and protein–nucleic acid …
ProTherm, version 4.0: thermodynamic database for proteins and mutants
KA Bava, MM Gromiha, H Uedaira… - Nucleic acids …, 2004 - academic.oup.com
Abstract Release 4.0 of ProTherm, thermodynamic database for proteins and mutants,
contains∼ 14 500 numerical data (∼ 450% of the first version) of several thermodynamic …
contains∼ 14 500 numerical data (∼ 450% of the first version) of several thermodynamic …
ThermoMutDB: a thermodynamic database for missense mutations
Proteins are intricate, dynamic structures, and small changes in their amino acid sequences
can lead to large effects on their folding, stability and dynamics. To facilitate the further …
can lead to large effects on their folding, stability and dynamics. To facilitate the further …
DbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications
Protein modification is an extremely important post-translational regulation that adjusts the
physical and chemical properties, conformation, stability and activity of a protein; thus …
physical and chemical properties, conformation, stability and activity of a protein; thus …