Primary structure of the hydrophobic plant protein crambin

Journal/Book: Biochemistry 20 (19), 5437-5443. 1981;

Abstract: Crambin, a hydrophobic plant seed protein, consists of a single chain of46 amino acids with a calculated molecular weight of 4720. The primarystructure was determined by using solid-phase sequencing techniques andwas confirmed through X-ray crystallographic analysis of the protein at1.5-A resolution (Hendrickson, W. A., & Teeter, M. M. (1981) Nature(London) 290, 107-112). High-performance liquid chromatographicseparation of the proteolytic fragments from crambin led to theidentification of two sites of microheterogeneity. The three disulfidebonds were located at positions 3-40, 4-32, and 16-26 from thecrystallographic data. Comparison of the primary structure with knownsequences revealed that crambin is homologous with the plant toxinspurothionin and viscotoxin. Methods to estimate protein secondarystructure were applied and found to predict all of crambin's structureexcept its amphiphilic helix. Author.

Keyword(s): AMINO-ACID-SEQUENCE

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