H-bonding mediates polarization of peptide groups in folded proteins.
The carbon-nitrogen J-couplings in the hydrogen bonding chains of proteins show that H-bonding mediates peptide-group polarization, which results in the general reduction of peptide-group polarity of folded proteins in solution. The net effect is to make large regions of protein secondary structure, especially beta-sheets, intrinsically more hydrophobic, contributing thereby to overall stability of the tertiary structure.
Department of Biochemistry and Molecular Biology, Mayo Graduate School, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA. juranic.nenad@mayo.edu
Nenad
N
Juranić
Slobodan
S
Macura
Franklyn G
FG
Prendergast
D000818:Animals; D002347:Carps; D002352:Carrier Proteins / Q000737:chemistry*; D004563:Electrochemistry; D050556:Fatty Acid-Binding Proteins; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010320:Parvalbumins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D051381:Rats; D025801:Ubiquitin / Q000737:chemistry*
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D010320:Parvalbumins; D010455:Peptides; D025801:Ubiquitin