01837nas a2200217   4500008004100000022001400041245008900055210006900144260000800213300001100221490000800232520109800240653003301338653002401371653002701395653001701422653002301439100001901462700002401481856011401505       2022                        eng d  a0301-462200aNative state conformational heterogeneity in the energy landscape of protein folding0 aNative state conformational heterogeneity in the energy landscap  cAPR  a1067610 v2833 aThe native structure of proteins is central to various functions performed by cells. A vital part of the structure-function paradigm of proteins is their inherent flexibility and dynamics. The dynamic interconversion between the conformational substates in the heterogeneous native state basin of the energy landscape enables a single protein molecule to perform multiple functions. The dynamics among the substates are assisted by the motion of different structural elements of a protein out of which side-chains of amino acids hold a significant position due to their involvement in various functions such as molecular recognition and dynamic allostery. This review briefly describes the origin of conformational heterogeneity in the native state ensemble and the motions of different structural modules that assist the equilibrium dynamics of the conformational substates. The review then centers the discussion on conformational heterogeneity due to side-chain movements in proteins, the experimental methods to detect and characterize them and their role in performing multiple functions.10aConformational heterogeneity10aDry molten globules10aEnergy landscape model10aNative state10aSide-chain packing1 aMishra, Prajna1 aJha, Santosh, Kumar  uhttps://library.ncl.res.in/content/native-state-conformational-heterogeneity-energy-landscape-protein-folding