Home LiteratureArticle Details
PMID: 9138588 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Modification of calcite crystal growth by abalone shell proteins: an atomic force microscope study.

Biophysical journal ·Vol. 72 ·No. 3 ·1997-03-00 ·Pages 1425-33

Walters DA, Smith BL, Belcher AM, Paloczi GT, Stucky GD, Morse DE, Hansma PK

Abstract

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.

MeSH Terms
Animals Calcium Carbonate/chemistry Crystallization Magnesium Microscopy, Atomic Force/methods Mollusca Proteins/isolation & purification,ultrastructure
Chemicals
Proteins Calcium Carbonate Magnesium
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Walters D A
Department of Physics, University of California, Santa Barbara 93106, USA. deronwal@physics.ucsb.edu
Smith B L
Belcher A M
Paloczi G T
Stucky G D
Morse D E
Hansma P K
References (11)
11 references, click to expand
  1. Atomic force microscopy of insulin single crystals: direct visualization of molecules and crystal growth.
    Biophys J. 1996 Aug;71(2):1071-8 PMID: 8842243
  2. Applications for atomic force microscopy of DNA.
    Biophys J. 1995 May;68(5):1672-7 PMID: 7612809
  3. Mechanisms of growth for protein and virus crystals.
    Nat Struct Biol. 1995 Nov;2(11):956-9 PMID: 7583668
  4. Protein tracking and detection of protein motion using atomic force microscopy.
    Biophys J. 1996 May;70(5):2421-31 PMID: 9172768
  5. Atomic force microscopy and molecular modeling of protein and peptide binding to calcite.
    Calcif Tissue Int. 1994 Feb;54(2):133-41 PMID: 8012868
  6. Urinary calcium oxalate crystal growth inhibitors.
    J Am Soc Nephrol. 1994 Nov;5(5 Suppl 1):S46-53 PMID: 7873744
  7. Probing oscillatory hydration potentials using thermal-mechanical noise in an atomic-force microscope.
    Phys Rev B Condens Matter. 1995 Sep 15;52(12):R8692-R8695 PMID: 9979928
  8. Analysis of the soluble organic matrix of five morphologically different kidney stones. Evidence for a specific role of albumin in the constitution of the stone protein matrix.
    Urol Res. 1995;23(1):45-51 PMID: 7618235
  9. Crystal tectonics: construction of reticulated calcium phosphate frameworks in bicontinuous reverse microemulsions.
    Science. 1994 Jun 10;264(5165):1576-8 PMID: 17769602
  10. Mechanisms of protein crystal growth: An atomic force microscopy study of canavalin crystallization.
    Phys Rev Lett. 1995 Oct 2;75(14):2774-2777 PMID: 10059401
  11. Biological control of crystal texture: a widespread strategy for adapting crystal properties to function.
    Science. 1993 Feb 5;259(5096):776-9 PMID: 17809339
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1997-03-00
Pages
1425-33
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1184525
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com