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Journal of Chemical Information and Computer Sciences|September 23, 2003
Importance of native-state topology for determining the folding rate of two-state proteinsM Michael GromihaBiophysical Chemistry|May 3, 2003
Influence of cation-pi interactions in different folding types of membrane proteinsM Michael GromihaJournal of Biotechnology|April 13, 2005
Influence of DNA stiffness in protein-DNA recognitionM Michael GromihaJournal of Chemical Information and Modeling|April 6, 2005
A statistical model for predicting protein folding rates from amino acid sequence with structural class informationM Michael GromihaBiophysical Chemistry|May 21, 2005
Motifs in outer membrane protein sequences: applications for discriminationM Michael GromihaJournal of Chemical Information and Modeling|April 3, 2009
Multiple contact network is a key determinant to protein folding ratesM Michael GromihaAnalytical Biochemistry|September 3, 2010
Influence of long-range contacts and surrounding residues on the transition state structures of proteinsM Michael GromihaBiopolymers|March 14, 2009
Revisiting "reverse hydrophobic effect": applicable only to coil mutations at the surfaceM Michael GromihaBiochimica Et Biophysica Acta|September 12, 2006
Influence of amino acid properties for discriminating outer membrane proteins at better accuracyM Michael Gromiha, Makiko SuwaBioinformatics (Oxford, England)|June 21, 2002
NETASA: neural network based prediction of solvent accessibilityShandar Ahmad, M Michael GromihaPageof 36