About: Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis

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About: Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis Goto Sponge NotDistinct Permalink

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scientific article published on 01 August 1995

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1995 (uk) article scientifique publié en 1995 (fr) artículu científicu espublizáu n'agostu de 1995 (ast) scientific article published on 01 August 1995 (en) im August 1995 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q72008833-AF386E67-DD6C-4758-94CB-5A491441A59A
publication date	1995-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q72008833-34E9D583-1519-4693-B218-A341E5F776F6
language of work or name	English
author name string	wds:Q72008833-01F6A8E8-9C28-4F9C-9447-7FE7996ECA5B wds:Q72008833-32BDCEC7-065D-4E41-99DD-2BD972B7AC18 wds:Q72008833-37625A64-587D-4835-847B-EBAE60FE0135 wds:Q72008833-4964CB6F-DC1B-444F-9193-A3E3C890E7C7 wds:Q72008833-531B7256-A5BE-4D81-8A57-A43916A8D85E wds:Q72008833-BE5F52C5-8217-44B7-93F8-ADF95EDB3A09
author name string	J M Hadden D Chapman I H van Stokkum M Bloemendal P I Haris H Linsdell
rdfs:label	Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (en) Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (nl)
skos:prefLabel	Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (en) Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (nl)
name	Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (en) Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (nl)
title	wds:Q72008833-07B27787-6582-4F0D-B08F-81A31487EF08
title	Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis (en)
page(s)	wds:Q72008833-0B67BC6C-3E61-4FFF-9725-EE1FB2D48581
page(s)	10508-10518
instance of	wds:Q72008833-135463D6-4048-45DD-8C9D-C07196DB5405
instance of	scholarly article
main subject	wds:Q72008833-11926505-91A0-45E4-95F3-0F5CBD8590BC
main subject	infrared spectroscopy
PubMed ID	wds:Q72008833-8ADDAE6E-4B28-40C2-9065-AADEE101A179
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7654705
PubMed ID	7654705
published in	wds:Q72008833-6961F4E3-1614-406A-AE8A-DD42350C04B8
published in	Biochemistry
issue	wds:Q72008833-3115C86A-4506-4F5E-81C0-7015878A729D
volume	wds:Q72008833-901FAA8B-E062-4716-8D94-3CFF046DDAC4
issue	33
volume	34
DOI	wds:Q72008833-2A67B90F-F45E-41EC-9BCB-BDAE5978710C
DOI	http://dx.doi.org/10.1021/BI00033A024
DOI	10.1021/BI00033A024
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q72008833
is cites work of	Secondary structure in lung surfactant SP-B peptides: IR and CD studies of bulk and monolayer phases Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra Immunohistowax processing, a new fixation and embedding method for light microscopy, which preserves antigen immunoreactivity and morphological structures: visualisation of dendritic cells in peripheral organs Membrane protein dynamics: limited lipid control. Probing the structure and dynamics of a DNA hairpin by ultrafast quenching and fluorescence depolarization Psychrophilic enzymes: a thermodynamic challenge Activation mechanism of recombinant Der p 3 allergen zymogen: contribution of cysteine protease Der p 1 and effect of propeptide glycosylation Interaction between soluble and membrane-embedded potassium channel peptides monitored by Fourier transform infrared spectroscopy A bacterial TrwC relaxase domain contains a thermally stable alpha-helical core. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media Structural characterization of IgG1 mAb aggregates and particles generated under various stress conditions Stability and folding dynamics of polyglutamic acid ESI-MS and FTIR studies of the interaction between the second PDZ domain of hPTP1E and target peptides Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study Structure and orientation of lung surfactant SP-C and L-alpha-dipalmitoylphosphatidylcholine in aqueous monolayers Heterogeneity in desiccated solutions: implications for biostabilization Frozen Microemulsions for MAPLE Immobilization of Lipase. Kinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin Thermodynamics of protein unfolding: questions pertinent to testing the validity of the two-state model. Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine alpha-lactalbumin: the stabilizing role of the calcium ion Reorientational dynamics of enzymes adsorbed on quartz: a temperature-dependent time-resolved TIRF anisotropy study Secondary structure, stability and tetramerisation of recombinant K(V)1.1 potassium channel cytoplasmic N-terminal fragment Correlation between thermal aggregation and stability of lysozyme with salts described by molar surface tension increment: an exceptional propensity of ammonium salts as aggregation suppressor Chronic liver and renal diseases differently affect structure of human serum albumin Pressure- and temperature-induced unfolding and aggregation of recombinant human interferon-gamma: a Fourier transform infrared spectroscopy study Thermal-induced dissociation and unfolding of homodimeric DsbC revealed by temperature-jump time-resolved infrared spectra Fucoidan as an inhibitor of thermally induced collagen glycation examined by acetate electrophoresis Investigations of intermediates appearing in the reassociation of the light-harvesting 1 complex of Rhodospirillum rubrum κ-Casein terminates casein micelle build-up by its "soft" secondary structure
is cites work of	wds:Q40119636-670E250E-B061-4390-83F3-4850AE383A4F wds:Q44518407-492F897E-6A83-4013-999F-DE20DD215DF6 wds:Q40285761-9FD00D5B-4780-4443-97E0-58EABE30222A wds:Q42928770-A91D077E-6473-4D9D-8C08-6AB6CB8CE14A wds:Q47282807-46AC02E5-6F3C-4EAA-9A16-03EE5E51A0E5 wds:Q78122762-A537F4C8-3241-4E56-BA25-8C48F0ED2560 wds:Q34473989-DF48D2D4-F633-4EFC-8021-B7ECEDF64F9F wds:Q63410467-A0566447-50DB-45D9-8189-6B31212577E7 wds:Q73705911-252BCDFA-973F-44A9-BE39-D5E68E5B00E0 wds:Q80337672-0D999F29-A735-4544-86C2-719DAB9CBD38 wds:Q41657470-D223B8BC-2A25-4D49-8401-5EE2653EC029 wds:Q28344541-7BBCB389-DDEF-4973-88D8-951F0ADFFC8F wds:Q87933367-CCA0FC7C-0AD0-482A-A5E3-2FAF4124C732 wds:Q33806048-EBFFE391-E349-4A48-9BF7-D1ACB780C395 wds:Q37418764-BCF45A3B-6084-4F2B-B0BA-D9FFEEE7713E wds:Q34989896-D08906CE-ACD4-41AA-A258-0F4F4DB51D99 wds:Q73614155-929D6501-2351-4F59-9F71-8D371D7D8BF2 wds:Q78673286-2F5F7D35-6F07-47FC-AE26-8AEAD61F7082 wds:Q87383274-7B0DEA36-0AD4-4391-B296-2C4B7D5C7AE7 wds:Q30366275-E26F4387-1E3C-4F58-BB2A-BDEC64CAAC04 wds:Q35996228-DA9E954D-AF44-4E59-9D8C-3A2CB4E6DAEF

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