Short hydrogen bonds in proteins.
Short hydrogen bonds are present in many chemical and biological systems. It is well known that these short hydrogen bonds are found in the active site of enzymes and aid enzyme catalysis. This study aims to systematically characterize all short hydrogen bonds from a nonredundant dataset of protein structures. The study has revealed that short hydrogen bonds are commonly found in proteins and are widely present in different regions of the protein chain, such as the backbone or side chain, and in different secondary structural regions such as helices, strands and turns. The frequency of occurrence of donors and acceptors from the charged side chains as well as from the neutral backbone atoms is equally high. This suggests that short hydrogen bonds in proteins occur either due to increased strength or due to geometrical constraints and this has been illustrated from several examples.
Rajagopal
Sathyapriya
S
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Vishveshwara
Saraswathi
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D019295:Computational Biology; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D033363:Neutron Diffraction; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D015203:Reproducibility of Results; D012984:Software; D055672:Static Electricity; D013455:Sulfur / Q000032:analysis / Q000737:chemistry
D000596:Amino Acids; D011506:Proteins; D013455:Sulfur