Coulombic interactions between partially charged main-chain atoms not hydrogen-bonded to each other influence the conformations of alpha-helices and antiparallel beta-sheet. A new method for analysing the forces between hydrogen bonding groups in proteins includes all the Coulombic interactions.
Maccallum, P H
Coulombic interactions between partially charged main-chain atoms not hydrogen-bonded to each other influence the conformations of alpha-helices and antiparallel beta-sheet. A new method for analysing the forces between hydrogen bonding groups in proteins includes all the Coulombic interactions. [electronic resource] - Journal of molecular biology Apr 1995 - 361-73 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/s0022-2836(95)80056-5 doi
Chemistry, Physical--methods
Computer Simulation
Hydrogen Bonding
Models, Molecular
Peptides--chemistry
Protein Structure, Secondary
Proteins--chemistry
Coulombic interactions between partially charged main-chain atoms not hydrogen-bonded to each other influence the conformations of alpha-helices and antiparallel beta-sheet. A new method for analysing the forces between hydrogen bonding groups in proteins includes all the Coulombic interactions. [electronic resource] - Journal of molecular biology Apr 1995 - 361-73 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/s0022-2836(95)80056-5 doi
Chemistry, Physical--methods
Computer Simulation
Hydrogen Bonding
Models, Molecular
Peptides--chemistry
Protein Structure, Secondary
Proteins--chemistry