Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units

Electrostatic interactions are of considerable importance in protein structure and function, and in a variety of cellular and biochemical processes. Here we report three similar findings from highly refined atomic structures of periplasmic binding proteins. Hydrogen bonds, acting primarily through b...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1987-10, Vol.329 (6139), p.561-564
Main Authors: Quiocho, F A, Sack, J S, Vyas, N K
Format: Article
Language:English
Subjects:
Amino Acids - metabolism
Arabinose - metabolism
Atoms & subatomic particles
Bacterial Proteins
Biochemistry
Carrier Proteins
Chemical Phenomena
Chemistry, Physical
Computer Graphics
energy charge
Hydrogen Bonding
Ions
Ligands
peptides
Protein Conformation
Proteins
Sulfates
Sulfates - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Electrostatic interactions are of considerable importance in protein structure and function, and in a variety of cellular and biochemical processes. Here we report three similar findings from highly refined atomic structures of periplasmic binding proteins. Hydrogen bonds, acting primarily through backbone peptide units, are mainly responsible for the involvement of the positively charged arginine 151 residue in the ligand site of the arabinose-binding protein, for the association between teh sulphate-binding protein and the completely buried sulphate dianion, and for the formation of the complex of the leucine/isoleucine/valine-binding protein with the leucine zwitterion. We propose a general mechanism in which the isolated charges on the various buried, desolvated ionic groups are stabilized by the polarized peptide units. This mechanism also has broad application to processes requiring binding of uncompensated ions and charged ligands and stabilization of enzyme reaction charged intermediates, as well as activation of catalytic residues.
ISSN:0028-0836
1476-4687
DOI:10.1038/329561a0