Ontology highlight
ABSTRACT:
SUBMITTER: Kleckner IR
PROVIDER: S-EPMC3061256 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Kleckner Ian R IR Foster Mark P MP
Biochimica et biophysica acta 20101106 8
Proteins are inherently flexible at ambient temperature. At equilibrium, they are characterized by a set of conformations that undergo continuous exchange within a hierarchy of spatial and temporal scales ranging from nanometers to micrometers and femtoseconds to hours. Dynamic properties of proteins are essential for describing the structural bases of their biological functions including catalysis, binding, regulation and cellular structure. Nuclear magnetic resonance (NMR) spectroscopy represe ...[more]