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The organic-mineral interaction in m...

Metzler, Rebecca A.

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The organic-mineral interaction in mollusk shell.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The organic-mineral interaction in mollusk shell./
作者:	Metzler, Rebecca A.
面頁冊數:	276 p.
附註:	Source: Dissertation Abstracts International, Volume: 71-10, Section: B, page: 5989.
Contained By:	Dissertation Abstracts International71-10B.
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3424026
ISBN:	9781124221014

The organic-mineral interaction in mollusk shell.
Metzler, Rebecca A.

The organic-mineral interaction in mollusk shell. - 276 p.

Source: Dissertation Abstracts International, Volume: 71-10, Section: B, page: 5989.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2010.

Macromolecules are a minority but important component of the minerals formed by living organisms, or biominerals. While many proteins from the nacre and prismatic layers of mollusk shells have been identified and sequenced, the molecular interaction, organization, and rearrangements of proteins upon organic-mineral bond formation, and the effect of this interaction on crystal formation, deformation, and orientation are poorly understood. To examine the organic-mineral interaction in mollusk shells, we prepared model systems consisting of calcium carbonate grown in the presence of synthetic mollusk shell polypeptides. X-ray absorption near-edge structure (XANES) spectroscopy and x-ray photoelectron emission microscopy (X-PEEM) were used to examine the electronic structure and bonding environment of both the surface and bulk of model biomineral crystals, thereby determining that the organic-mineral interaction is a series of events starting with bond formation and ending with the fully formed mineral.

ISBN: 9781124221014Subjects--Topical Terms:

518360
Biophysics.

The organic-mineral interaction in mollusk shell.
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500 $a Adviser: Pupa Gilbert.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2010.
520 $a Macromolecules are a minority but important component of the minerals formed by living organisms, or biominerals. While many proteins from the nacre and prismatic layers of mollusk shells have been identified and sequenced, the molecular interaction, organization, and rearrangements of proteins upon organic-mineral bond formation, and the effect of this interaction on crystal formation, deformation, and orientation are poorly understood. To examine the organic-mineral interaction in mollusk shells, we prepared model systems consisting of calcium carbonate grown in the presence of synthetic mollusk shell polypeptides. X-ray absorption near-edge structure (XANES) spectroscopy and x-ray photoelectron emission microscopy (X-PEEM) were used to examine the electronic structure and bonding environment of both the surface and bulk of model biomineral crystals, thereby determining that the organic-mineral interaction is a series of events starting with bond formation and ending with the fully formed mineral.
520 $a XANES spectra acquired from the model biomineral systems showed that upon organic-mineral bond formation both the crystal and the polypeptides exhibit bond and molecular structure alterations. We acquired XANES spectra from the surface of calcium carbonate crystals grown in the presence of six synthetic polypeptides sequenced after mollusk nacre proteins: AP7N, AP24N, N16N, asp1, asp2, and ACCN. All of these model biominerals gave similar results, namely the disruption of CO bonds in calcite and enhancement of the peaks associated with C-H bonds bonds in peptides, indicating disordering of the calcite crystal and ordering of the peptides upon binding. We also show that these changes do not occur when the acidic amino acids, Asp and Glu, are replaced in the N16N sequence with Asn and Gln, respectively, demonstrating the importance of carboxyl groups in organic-mineral bond formation.
520 $a We examined the bulk crystal structure of crystals grown in the presence of N16N and asp2 using XANES and X-PEEM. The experiments clearly show that asp2 is occluded in fully formed biomineral crystals, and slightly, but permanently disorders the crystal structure at short- and long-range distances. The N16N peptide self-assembles into regularly spaced layers and induces the formation of aragonite within these layers.
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