Peptide hydrogen bond

Guo, H., and M. Karplus. 1994. Solvent Influence on the Stability of the Peptide Hydrogen Bond A Supramolecular Cooperative Effect. J. Phys. Chem. 98, 7104-7105. 

Hydrogen bonding. Because peptide units form hydrogen bonds to water in the unfolded state, peptide-peptide hydrogen bonds must form in the folded state to avoid an otherwise intolerable loss of enthalpy (13). 

Stability of the Peptide Hydrogen Bond A Supramolecular Cooperative Effect. 

Many-Body Effects in Systems of Peptide Hydrogen- Bonded Networks and Their Gontributions to Ligand Binding A Comparison of DFT and Polarizable Molecular... 

Guo, H. and Karplus, M., Solvent influence on the stability of the peptide hydrogen bond A supramolecular cooperative effect, J. Phys. Chem. 98, 7104—7105 (1994). 

Crick (1954) proposed a two-stranded helix, somewhat reminiscent of the Watson-Crick double-strand helix which had been so successful for deoxyribonucleic acid. The model consisted of two polypeptide chains wound helically around a common axis and held together by interchain peptide hydrogen bonds. The peptide bonds were all in the cfs-configuration, and the repeating unit consisted of a pair of amino acid residues, one perpendicular and the other parallel to the fiber axis. As a result, planes... 

Baldwin RL (2003) In search of the energetic role of peptide hydrogen bonds. J Biol Chem 278 17581-17588... 

For oriented polypeptide chains, IR dichroism provides an informative technique. In a helix, N— 0=C peptide hydrogen bonds are oriented parallel to the long axis of the molecule. Therefore the N—H stretch and amide I bands should preferentially absorb IR radiation when the direction of polarization is parallel to the heUx axis. The amide II band should show the opposite trend. In p sheets, the long axis of the structure is along the extended peptide chains and the hydrogen bonds are perpendicular to this axis. Therefore each IR band in P sheets would have chroism opposite to that observed for the corresponding band in an a helix. 

Hanlon and Klotz (1968) have discussed the use of near-infrared spectroscopy for studying structural problems of biochemistry. In particular, they have considered the equilibrium state of the peptide unit in a number of synthetic polyamino acids (poly-L-alanine, poly-L-leucine, poly-L-methionine, and poly-y-benzyl-L-glutamate) as a function of solvent composition under conditions where the transitions in other physical properties of these polymers have been interpreted as simple peptide, hydrogen-bonded, helix-to-coil transitions. Their spectral data demonstrate that these conversions involve protonated peptide species and are far more complicated than investigators of these processes had assumed. 

Keywords Ferrocene Amino acid Peptide Hydrogen bond ... 

Many-body effects in systems of peptide hydrogen-bonded networks and their contributions to ligand binding A comparison of the performances of DFT and polarizable molecular mechanics ... 

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