Three-dimensional protein shape rendering in magnetized solution with Lambert-Beer law.
When monochromatic light passes through a homogeneous absorbing medium, the absorbance is proportional to the growth of concentration and thickness of the medium, which is the Lambert-Beer law. The shade selection of protein solution magnetized for a certain time from different angles makes different absorbance, which does not meet the Lambert-Beer law. Accordingly, we derive that the absorbance A is not only proportional to the concentration and thickness of the medium but also proportional to the light area S(S) of a certain direction. For the same protein solution, we can obtain the absorbance A of six directions and thus get six values for S(S) the relative ratio of which will inevitably reveal plentiful information of the protein shape. The conformation of the protein can be easily drawn out by software (MATLAB 7.0.1). We have drawn out the molecular shape of lysozyme and bovine serum albumin. In brief, we have developed the Lambert-Beer law A=K·C·b·S(s) and a new method of exploring protein spatial structure.
State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, TaiAn, Shandong 271018, China.
HongYan
H
Gu
WeiShan
W
Chang
D000042:Absorption; D000465:Algorithms; D000818:Animals; D002417:Cattle; D008027:Light; D060526:Magnetic Fields; D009113:Muramidase / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry; D012996:Solutions / Q000737:chemistry
D011506:Proteins; D012996:Solutions; D012710:Serum Albumin, Bovine; D009113:Muramidase