%0 Journal Article %T Investigation of the impact of PTMs on the protein backbone conformation %+ Biologie Intégrée du Globule Rouge (BIGR (UMR_S_1134 / U1134)) %+ The Scripps Research Institute [La Jolla, San Diego] %+ Institut National de la Transfusion Sanguine [Paris] (INTS) %+ Laboratoire d'Excellence : Biogenèse et pathologies du globule rouge (Labex Gr-Ex) %+ Department of Computer Science and Mathematics [Lebanese American University] (CSM/SAS/LAU) %A Craveur, Pierrick %A Narwani, Tarun %A Rebehmed, Joseph %A de Brevern, Alexandre %Z the Ministry of Research (France), %Z University de Paris, University Paris Diderot, Sorbonne, Paris Cité (France), %Z National Institute for Blood Transfusion (INTS, France), %Z National Institute for Health and Medical Research (INSERM, France), %Z French National Computing Centre CINES under grant no. c2013037147 by the GENCI (Grand Equipement National de Calcul Intensif). %Z Indo-French Centre for the Promotion of Advanced Research / CEFIPRA for collaborative grant (number 5302-2). %Z Calculations were also performed on an SGI cluster granted by Conseil Régional Ile de France and INTS (SESAME Grant) %< avec comité de lecture %@ 0939-4451 %J Amino Acids %I Springer Verlag %V 51 %N 7 %P 1065-1079 %8 2019-07 %D 2019 %Z 1908.05122 %R 10.1007/s00726-019-02747-w %M 31183539 %K rigidity %K mobility %K deformability %K N-glycosylation %K phosphorylation %K methylation %K statistics %K renin endopeptidase %K liver carboxylesterase %K cyclin-dependent kinase 2 (CDK2) %K actin %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology %Z Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Journal articles %X Post-Translational Modifications (PTMs) are known to play a critical role in the regulation of the protein functions. Their impact on protein structures, and their link to disorder regions have already been spotted on the past decade. Nonetheless, the high diversity of PTMs types, and the multiple schemes of protein modifications (multiple PTMs, of different types, at different time, etc) make difficult the direct confrontation of PTM annotations and protein structures data.We so analyzed the impact of the residue modifications on the protein structures at local level. Thanks to a dedicated structure database, namely PTM-SD, a large screen of PTMs have been done and analyze at a local protein conformation levels using the structural alphabet Protein Blocks (PBs). We investigated the relation between PTMs and the backbone conformation of modified residues, of their local environment, and at the level of the complete protein structure. The two main PTM types (N-glycosylation and phosphorylation) have been studied in non-redundant datasets, and then, 4 different proteins were focused, covering 3 types of PTMs: N-glycosylation in renin endopeptidase and liver carboxylesterase, phosphorylation in cyclin-dependent kinase 2 (CDK2), and methylation in actin. We observed that PTMs could either stabilize or destabilize the backbone structure, at a local and global scale, and that these effects depend on the PTM types. %G English %2 https://inserm.hal.science/inserm-02266176/document %2 https://inserm.hal.science/inserm-02266176/file/preprint_Craveur_Biochimie_2019-compres.pdf %L inserm-02266176 %U https://inserm.hal.science/inserm-02266176 %~ INSERM %~ UNIV-PARIS7 %~ UNIV-AG %~ AFRIQ %~ GENCI %~ USPC %~ UNIV-PARIS %~ UP-SCIENCES %~ ANR