Protein Engineering, Vol. 12, No. 12, 1063-1073,
December 1999
© 1999 Oxford University Press
Hidden Markov model approach for identifying the modular framework of the protein backbone
1 Équipe de Bioinformatique Moléculaire, INSERM U155, Université Paris VII, case 7113, 2 Place Jussieu, 75251 Paris Cedex 05 and 2 Département de Biomathématiques, CHU Pitié-Salpêtrière, 91 boulevard de l'Hôpital, 75013 Paris Cedex 13, France
The hidden Markov model (HMM) was used to identify recurrent short 3D structural building blocks (SBBs) describing protein backbones, independently of any a priori knowledge. Polypeptide chains are decomposed into a series of short segments defined by their inter-
-carbon distances. Basically, the model takes into account the sequentiality of the observed segments and assumes that each one corresponds to one of several possible SBBs. Fitting the model to a database of non-redundant proteins allowed us to decode proteins in terms of 12 distinct SBBs with different roles in protein structure. Some SBBs correspond to classical regular secondary structures. Others correspond to a significant subdivision of their bounding regions previously considered to be a single pattern. The major contribution of the HMM is that this model implicitly takes into account the sequential connections between SBBs and thus describes the most probable pathways by which the blocks are connected to form the framework of the protein structures. Validation of the SBBs code was performed by extracting SBB series repeated in recoding proteins and examining their structural similarities. Preliminary results on the sequence specificity of SBBs suggest promising perspectives for the prediction of SBBs or series of SBBs from the protein sequences.
Keywords: Markov chain/pattern classification/protein backbone/protein conformation/protein structure
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