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2016 ; 12
(12
): 1084-1088
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A prevalent intraresidue hydrogen bond stabilizes proteins
#MMPMID27748749
Newberry RW
; Raines RT
Nat Chem Biol
2016[Dec]; 12
(12
): 1084-1088
PMID27748749
show ga
Current limitations in de novo protein structure prediction and design suggest an
incomplete understanding of the interactions that govern protein folding. Here we
demonstrate that previously unappreciated hydrogen bonds occur within proteins
between the amide proton and carbonyl oxygen of the same residue. Quantum
calculations, infrared spectroscopy, and nuclear magnetic resonance spectroscopy
show that these interactions share hallmark features of canonical hydrogen bonds.
Biophysical analyses demonstrate that selective attenuation or enhancement of
these C5 hydrogen bonds affects the stability of synthetic ?-sheets. These
interactions are common, affecting approximately 5% of all residues and 94% of
proteins, and their cumulative impact provides several kilocalories per mole of
conformational stability to a typical protein. C5 hydrogen bonds especially
stabilize the flat ?-sheets of the amyloid state, which is linked with
Alzheimer's disease and other neurodegenerative disorders. Inclusion of these
interactions in computational force fields would improve models of protein
folding, function, and dysfunction.
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