Walters D A, Smith B L, Belcher A M, Paloczi G T, Stucky G D, Morse D E, Hansma P K
Department of Physics, University of California, Santa Barbara 93106, USA.
Biophys J. 1997 Mar;72(3):1425-33. doi: 10.1016/S0006-3495(97)78789-7.
A family of soluble proteins from the shell of Haliotis rufescens was introduced over a growing calcite crystal being scanned in situ by an atomic force microscope (AFM). Atomic step edges on the crystal surface were altered in shape and speed of growth by the proteins. Proteins attached nonuniformly to the surface, indicating different interactions with crystallographically different step edges. The observed changes were consistent with the habit modification induced by this family of proteins, as previously observed by optical microscopy. To facilitate further studies in this area, AFM techniques and certain AFM imaging artifacts are discussed in detail.
将来自红鲍贝壳的一族可溶性蛋白质引入到一个正在通过原子力显微镜（AFM）进行原位扫描的方解石生长晶体上。晶体表面的原子台阶边缘在形状和生长速度上因这些蛋白质而发生改变。蛋白质在表面的附着不均匀，这表明与晶体学上不同的台阶边缘存在不同的相互作用。观察到的这些变化与此前通过光学显微镜观察到的由该族蛋白质诱导的习性改变是一致的。为便于在该领域开展进一步研究，详细讨论了AFM技术及某些AFM成像假象。
