Kuwata K, Hoshino M, Forge V, Era S, Batt C A, Goto Y
Department of Physiology, School of Medicine, Gifu University, Tsukasamachi, Japan.
Protein Sci. 1999 Nov;8(11):2541-5. doi: 10.1110/ps.8.11.2541.
Using heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel beta-barrel and one major alpha-helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including betaI-strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried under the major alpha-helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions.
我们使用异核核磁共振光谱研究了牛β-乳球蛋白A在pH 2.0和45℃下的溶液结构和动力学，此时该蛋白质以单体天然状态存在。单体核磁共振结构由一个八链连续反平行β-桶和一个主要的α-螺旋组成，与在pH 6.2时获得的X射线二聚体结构相似，包括形成二聚体界面的βI链和作为内部疏水孔盖子的环EF。[1H]-15N NOE表明，埋在主要α-螺旋下的βF、βG和βH链在皮秒到纳秒的时间尺度上是刚性的，同时也强调了环以及N端和C端区域的快速波动。
