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Backbone structure and dynamics of a hemolymph protein from the mealworm beetle Tenebrio molitor



Backbone structure and dynamics of a hemolymph protein from the mealworm beetle Tenebrio molitor



Biochemistry 36(45): 13791-13801



Pheromones play a vital role in the survival of insects and are used for chemical communication between members of the same species by their olfactory system. The selection and transportation of these lipophilic messengers by carrier proteins through the hydrophilic sensillum lymph in the antennae toward their membrane receptors remains the initial step for the signal transduction pathway. A moderately abundant 12.4 kDa hydrophilic protein present in hemolymph from the mealworm beetle Tenebrio molitor is approximately 38% identical to a family of insect pheromone-binding proteins. The backbone structure and dynamics of the 108-residue protein have been characterized using three-dimensional 1H-15N NMR spectroscopy, combined with 15N relaxation and 1H/D exchange measurements. The secondary structure, derived from characteristic patterns of dipolar connectivities between backbone protons, secondary chemical shifts, and homonuclear three-bond JHNH alpha coupling constants, consists of a predominantly disordered N-terminus from residues 1 to 10 and six alpha-helices connected by four 4-7 residue loops and one beta-hairpin structure. The up-and-down arrangement of alpha-helices is stabilized by two disulfide bonds and hydrophobic interactions between amphipathic helices. The backbone dynamics were characterized by the overall correlation time, order parameters, and effective correlation times for internal motions. Overall, a good correlation between secondary structure and backbone dynamics was found. The 15N relaxation parameters T1 and T2 and steady-state NOE values of the six alpha-helices could satisfactorily fit the Lipari-Szabo model. In agreement with their generalized order parameters (> 0.88), residues in helical regions exhibited restricted motions on a picosecond time scale. The stability of this highly helical protein was confirmed by thermal denaturation studies.

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Accession: 008210300

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PMID: 9374855

DOI: 10.1021/bi971529k


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