title: Statistical characterization of salt bridges in proteins.
abstract: The structure and folding mechanism of a given protein are determined by many factors, including the electrostatic interactions between charged residues of protein molecules known in general as salt bridges. In this study, analyses were conducted on 10,370 salt bridges in 2017 proteins and the results compared to previous statistical surveys of 36 protein structures. Although many of the general trends remained consistent with other studies, more detailed information was illuminated by the larger dataset. In particular, it was shown that there is a strong correlation between secondary structure and salt bridge formation, and that salt bridges display preferential formation in an environment of about 30% solvent accessible surface area.
authors: Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, USA.
authors: James N
authors: JN
authors: Sarakatsannis
authors: Yong
authors: Y
authors: Duan
mesh_terms: D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D001665:Binding Sites; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012492:Salts; D012997:Solvents; D013499:Surface Properties
chemical_list: D000596:Amino Acids; D011506:Proteins; D012492:Salts; D012997:Solvents