Modification of calcite crystal growth by abalone shell proteins: an atomic force microscope study.
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.
Walters
D A
DA
Department of Physics, University of California, Santa Barbara 93106, USA. deronwal@physics.ucsb.edu
Smith
B L
BL
Belcher
A M
AM
Paloczi
G T
GT
Stucky
G D
GD
Morse
D E
DE
Hansma
P K
PK
D000818:Animals; D002119:Calcium Carbonate / Q000737:chemistry*; D003460:Crystallization; D008274:Magnesium; D018625:Microscopy, Atomic Force / Q000379:methods; D008974:Mollusca; D011506:Proteins / Q000302:isolation & purification / Q000648:ultrastructure
D011506:Proteins; D002119:Calcium Carbonate; D008274:Magnesium