Selective absorption of radio frequency energy due to collective motion of charged domains: case of lysozyme crystal.
A new aspect of the internal protein motion is pointed-- the electrostatic charges of the titratable groups fixed on the protein structure are combined with the hinge binding motion of lysozyme domain. Then the lysozyme molecule is examined as a system having charges that oscillate with the parameters of the mechanical motion. So, from such point of view, the lysozyme molecule becomes infrared and radiofrequency active. This model is applied for the case of a triclinic lysozyme crystal and the direction of the external electromagnetic flux in respect to the main crystal axes is found that corresponds to the best conditions for maximal absorption. For the purpose of the experimental measurement of the space dependence of the absorption, the direction of the incident wave and its polarization are calculated in respect to the main crystal planes in case of maximal efficiency of the absorption.
Alexov
E
E
Institute of Organic Chemistry Bulgarian Academy of Sciences, Sofia, Bulgaria.
Atanasov
B
B
D000042:Absorption; D003460:Crystallization; D007477:Ions; D009038:Motion; D009113:Muramidase / Q000737:chemistry / Q000528:radiation effects*; D017434:Protein Structure, Tertiary; D011846:Radio Waves; D013314:Stress, Mechanical; D013816:Thermodynamics; D017186:Titrimetry
D007477:Ions; D009113:Muramidase