SMALL-ANGLE X-RAY-SCATTERING STUDIES OF THE C-HORDEINS OF BARLEY (HORDEUM-VULGARE)

被引:24
作者
IANSON, KJ
MORRIS, VJ
SHEWRY, PR
TATHAM, AS
机构
[1] UNIV BRISTOL, INST ARABLE CROPS RES, LONG ASHTON RES STN, BRISTOL BS18 9AF, AVON, ENGLAND
[2] INST FOOD RES, NORWICH LAB, NORWICH NR4 7UA, NORFOLK, ENGLAND
关键词
D O I
10.1042/bj2870183
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Small angle X-ray scattering was used to study the solution conformation of the C hordeins of barley (Hordeum vulgare), a group of proteins whose primary structure consists predominantly of an octapeptide repeat motif. Measurements on the protein in 0.1 m-acetic acid at 25-degrees-C are consistent with a model for the protein conformation of a stiff coil, the so-called 'worm-like' chain. The characteristic parameters (the Kuhn statistical segment length and the contour length) of the protein were calculated as 5.11 and 71.5 nm respectively.
引用
收藏
页码:183 / 185
页数:3
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