About: Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels

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About: Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 2000

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 2000 (uk) im Oktober 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 2000 (ast) scientific article published on 01 October 2000 (en)
publication date	wds:Q73081771-98056D88-9627-4318-9567-ADA4C3CA33D0
publication date	2000-10-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q73081771-0B732EE2-4E56-48D8-9C0E-E0D38904D158 wds:Q73081771-3029FBCD-C6F3-4BE4-ABD5-12C75765DB42 wds:Q73081771-3B21AB04-134A-478C-B7D9-13040D10008E wds:Q73081771-5FEB1195-6A83-427B-A803-4D579B756037 wds:Q73081771-70F78407-06DD-45AC-817A-93253F525AF1 wds:Q73081771-8FC25504-C167-4D73-B739-AB2AAE184F71 wds:Q73081771-A488CE9A-B488-4024-9F63-F6EC85A1DF8A wds:Q73081771-AF19BC0D-A0EA-498F-A2EB-983BC7E2F662 wds:Q73081771-B6A9668F-AC05-4136-B27C-642EC1661747 wds:Q73081771-BF2D8CE5-E871-4EF0-8BD8-927A4C224306 wds:Q73081771-DED3BA6A-6D46-4799-BE85-F7B7C7857913
cites work	Examination of the secondary structure of proteins by deconvolved FTIR spectra Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis Partially folded structure of monomeric bovine β-lactoglobulin The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein New insight into protein secondary structure from resolution-enhanced infrared spectra Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution A model for the denaturation and aggregation of beta-lactoglobulin. The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin Thermodenaturation of bovine -lactoglobulin. Kinetics and the introduction of -structure Fine-stranded and particulate gels of β-lactoglobulin and whey protein at varying pH Gelation of proteins from milk.
author name string	wds:Q73081771-0ED44778-8D72-48A3-899A-1F517CC5436C wds:Q73081771-394F58AE-77ED-454D-BB4F-6E50AF59FC34 wds:Q73081771-F8D8D969-4ACF-4839-9435-94D744FE8E0A
author name string	G M Kavanagh S B Ross-Murphy A H Clark
rdfs:label	Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (en) Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (nl)
skos:prefLabel	Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (en) Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (nl)
name	Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (en) Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (nl)
title	wds:Q73081771-681FFFFF-2738-4E15-9D45-2D9AB8EBAD4F
title	Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH beta-lactoglobulin gels (en)
page(s)	wds:Q73081771-3F159AB1-D0FA-45F9-9C23-3E7A516520C3
page(s)	41-50
instance of	wds:Q73081771-7BC09E9B-06AF-4489-BE4C-79CF2D3B25CE
instance of	scholarly article
PubMed ID	wds:Q73081771-4211241C-ACD5-4F56-B9C3-03BB54D27744
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11033176
PubMed ID	11033176
published in	wds:Q73081771-B8B1CF9C-84D7-456E-8D2D-CCAB5A111113
published in	International Journal of Biological Macromolecules
issue	wds:Q73081771-48E9B30A-98B6-4F4C-8906-AF2B585B95E5
volume	wds:Q73081771-110DC050-0783-4C6F-958A-1651116728F1
issue	1
volume	28
DOI	wds:Q73081771-2F98A7DB-3329-4881-A3D1-FCACC39D56B9
DOI	http://dx.doi.org/10.1016/S0141-8130(00)00144-6
DOI	10.1016/S0141-8130(00)00144-6
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73081771
is cites work of	Thermally induced fibrillar aggregation of hen egg white lysozyme A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea Understanding amyloid aggregation by statistical analysis of atomic force microscopy images Sonication of proteins causes formation of aggregates that resemble amyloid Rheological properties of peptide-based hydrogels for biomedical and other applications Determination and Quantification of Molecular Interactions in Protein Films: A Review Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean). Thermal aggregation and ion-induced cold-gelation of bovine serum albumin Flow-assisted assembly of nanostructured protein microfibers Protein-Based Nanostructures for Food Applications Rheological properties and microstructure of xylanase containing whole wheat bread dough Composite Gels Containing Whey Protein Fibrils and Bacterial Cellulose Microfibrils Impact of stirring speed on β-lactoglobulin fibril formation
is cites work of	wds:Q30849505-3D3AA2B4-BE4F-4A0A-9D5C-16DB4F98840D wds:Q42321755-401A3659-A888-400C-85FF-CF10ADB2B8B4 wds:Q40312596-CAD21B2E-26BB-42B7-8315-A88ADAF4BFBF wds:Q64111156-8F7227C5-1E02-43AB-968F-74EFD48C36FB wds:Q83163280-7693065B-59D3-4F81-9C74-AC21E13FE656 wds:Q91639653-81EEBF5B-3E5C-426A-9035-1D636A5BF6E1 wds:Q30329217-3FB5FAE2-F798-4EAC-A463-91B21CA8B254 wds:Q42078881-85F811DC-5928-4C24-9CBC-FF59830C6BF5 wds:Q91831615-7D5D9A23-A3D2-4F6E-A478-34DF3A404D4A wds:Q35016082-073C3821-D707-4742-9CAF-90850DA29140 wds:Q84039071-CE25C0C5-3200-4FA3-8B26-F4E317FCD73D wds:Q38673122-4F308D9A-1395-4B17-B769-34D722ED8EEF wds:Q41984384-F19F7AE2-B5C4-47C1-94B3-0CA60EE43474

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