A study on chirality in biomolecules: the effect of the exchange of L: amino acids to D: ones in Sso7d ribonuclease.
In this work, the conformational behavior of ribonuclease Sso7d is studied as a function of chirality of its constituting amino acids. Both optimized structures (using molecular mechanics with the CHARMM force field) and dynamic behavior (obtained by molecular dynamic simulations) are compared.
Ladik
János J
JJ
Chair for Theoretical Chemistry and Laboratory of the National Foundation for Cancer Research, Friedrich-Alexander-University-Erlangen, Nürnberg, Egerlandstrasse 3, D-91058, Erlangen, Germany. janos.ladik@chemie.uni-erlangen.de
Szekeres
Zsolt
Z
D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012260:Ribonucleases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D013237:Stereoisomerism; D040681:Structural Homology, Protein
D000596:Amino Acids; D012260:Ribonucleases