X-ray analysis of new crystal forms of the sweet protein thaumatin.
Identifieur interne : 000533 ( Main/Exploration ); précédent : 000532; suivant : 000534X-ray analysis of new crystal forms of the sweet protein thaumatin.
Auteurs : A. Mcpherson [États-Unis] ; J. WeickmannSource :
- Journal of biomolecular structure & dynamics [ 0739-1102 ] ; 1990.
Descripteurs français
- KwdFr :
- MESH :
- ultrastructure : Protéines végétales.
- Conformation des protéines, Cristallisation, Diffraction des rayons X, Édulcorants.
English descriptors
- KwdEn :
- MESH :
- chemical , ultrastructure : Plant Proteins.
- Crystallization, Protein Conformation, Sweetening Agents, X-Ray Diffraction.
Abstract
Thaumatin is a plant protein that in the mature form contains 8 disulfide bonds and 207 amino acids. Several forms of this protein occur naturally and each elicits an intense sweetness sensation when tasted in microgram quantities. The two major forms of thaumatin are easily separable by ion exchange chromatography. Crystals of the two proteins (designated here A and B) have been grown by vapor equilibration from solutions containing polyethylene glycol and examined by X-ray diffraction. The thaumatin A crystals are of space group P2(1)2(1)2(1) with a = 44.3 A, b = 63.7 A and c = 72.7 A. The crystals of thaumatin B are of space group C2 with a = 117.7 A, b = 44.9 A, and c = 38.0 A and beta = 94.0 degrees. Both crystals diffract to well beyond 2.3 A and appear suitable for high resolution structure analysis. Four heavy atom derivatives of thaumatin B have been generated and diffraction data to 4 A resolution have been collected. This work is designed to provide a basis for studying the 3-dimensional structure of more than 100 genetically generated thaumatin derivatives, several of which show enhanced stability and improved taste characteristics.
DOI: 10.1080/07391102.1990.10508545
PubMed: 2360997
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Weickmann</name></author></analytic><series><title level="j">Journal of biomolecular structure & dynamics</title><idno type="ISSN">0739-1102</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization (MeSH)</term><term>Plant Proteins (ultrastructure)</term><term>Protein Conformation (MeSH)</term><term>Sweetening Agents (MeSH)</term><term>X-Ray Diffraction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Cristallisation (MeSH)</term><term>Diffraction des rayons X (MeSH)</term><term>Protéines végétales (ultrastructure)</term><term>Édulcorants (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallization</term><term>Protein Conformation</term><term>Sweetening Agents</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallisation</term><term>Diffraction des rayons X</term><term>Édulcorants</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thaumatin is a plant protein that in the mature form contains 8 disulfide bonds and 207 amino acids. Several forms of this protein occur naturally and each elicits an intense sweetness sensation when tasted in microgram quantities. The two major forms of thaumatin are easily separable by ion exchange chromatography. Crystals of the two proteins (designated here A and B) have been grown by vapor equilibration from solutions containing polyethylene glycol and examined by X-ray diffraction. The thaumatin A crystals are of space group P2(1)2(1)2(1) with a = 44.3 A, b = 63.7 A and c = 72.7 A. The crystals of thaumatin B are of space group C2 with a = 117.7 A, b = 44.9 A, and c = 38.0 A and beta = 94.0 degrees. Both crystals diffract to well beyond 2.3 A and appear suitable for high resolution structure analysis. Four heavy atom derivatives of thaumatin B have been generated and diffraction data to 4 A resolution have been collected. This work is designed to provide a basis for studying the 3-dimensional structure of more than 100 genetically generated thaumatin derivatives, several of which show enhanced stability and improved taste characteristics.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">2360997</PMID><DateCompleted><Year>1990</Year><Month>08</Month><Day>06</Day></DateCompleted><DateRevised><Year>2003</Year><Month>11</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0739-1102</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>5</Issue><PubDate><Year>1990</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of biomolecular structure & dynamics</Title><ISOAbbreviation>J Biomol Struct Dyn</ISOAbbreviation></Journal><ArticleTitle>X-ray analysis of new crystal forms of the sweet protein thaumatin.</ArticleTitle><Pagination><MedlinePgn>1053-60</MedlinePgn></Pagination><Abstract><AbstractText>Thaumatin is a plant protein that in the mature form contains 8 disulfide bonds and 207 amino acids. Several forms of this protein occur naturally and each elicits an intense sweetness sensation when tasted in microgram quantities. The two major forms of thaumatin are easily separable by ion exchange chromatography. Crystals of the two proteins (designated here A and B) have been grown by vapor equilibration from solutions containing polyethylene glycol and examined by X-ray diffraction. The thaumatin A crystals are of space group P2(1)2(1)2(1) with a = 44.3 A, b = 63.7 A and c = 72.7 A. The crystals of thaumatin B are of space group C2 with a = 117.7 A, b = 44.9 A, and c = 38.0 A and beta = 94.0 degrees. Both crystals diffract to well beyond 2.3 A and appear suitable for high resolution structure analysis. Four heavy atom derivatives of thaumatin B have been generated and diffraction data to 4 A resolution have been collected. 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Weickmann</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Mcpherson, A" sort="Mcpherson, A" uniqKey="Mcpherson A" first="A" last="Mcpherson">A. Mcpherson</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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