Editing Structural bioinformatics (section)

=== Interactions ===
Interactions are contacts established between parts of molecules at different levels. They are responsible for stabilizing protein structures and perform a varied range of activities. In [[biochemistry]], interactions are characterized by the proximity of atom groups or molecules regions that present an effect upon one another, such as [[electrostatic forces]], [[hydrogen bond]]ing, and [[hydrophobic effect]]. Proteins can perform several types of interactions, such as [[Protein–protein interaction|protein-protein interactions (PPI)]], protein-peptide interactions'''<ref>{{cite journal | vauthors = Stanfield RL, Wilson IA | title = Protein-peptide interactions | journal = Current Opinion in Structural Biology | volume = 5 | issue = 1 | pages = 103–13 | date = February 1995 | pmid = 7773739 | doi = 10.1016/0959-440X(95)80015-S }}</ref>''', protein-ligand interactions (PLI)'''<ref>{{cite book|title=Drug Design|vauthors=Klebe G|date=2015|publisher=Springer|isbn=978-3-642-17906-8|veditors=Scapin G, Patel D, Arnold E|series=NATO Science for Peace and Security Series A: Chemistry and Biology|location=Dordrecht|pages=83–92|chapter=Protein–Ligand Interactions as the Basis for Drug Action|doi=10.1007/978-3-642-17907-5_4}}</ref>''', and protein-DNA interaction.[[File:Contacts between two amino acid residues- Q196-R200 (PDB ID- 2X1C).png|thumb|Contacts between two amino acid residues: Q196-R200 (PDB ID- 2X1C)<ref>{{Cite web|url=http://proteus.dcc.ufmg.br/|title=Proteus {{!}} PROTein Engineering Supporter {{!}}|website=proteus.dcc.ufmg.br|access-date=2020-02-26}}</ref>|alt=|right]]