About: A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions

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About: A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions Goto Sponge NotDistinct Permalink

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scientific article published on 01 March 1992

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 1992 (uk) artículu científicu espublizáu en marzu de 1992 (ast) im März 1992 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 March 1992 (en)
publication date	wds:Q68127905-2D7B1C41-DBDF-4EE8-A242-1DF83548DFDF
publication date	1992-03-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q68127905-67B91D18-18AF-4DDF-B5A0-0C9FA2E171E3 wds:Q68127905-8D61C6AF-0BED-4702-ACFE-24142CC3E67A
author name string	H Saitô M Yokoi
rdfs:label	A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (en) A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (nl)
skos:prefLabel	A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (en) A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (nl)
name	A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (en) A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (nl)
title	wds:Q68127905-8472E48A-0736-468C-B290-70C300B027C0
title	A 13C NMR study on collagens in the solid state: hydration/dehydration-induced conformational change of collagen and detection of internal motions (en)
page(s)	wds:Q68127905-8AD37FD5-1B21-49D4-BBED-7C8983C1FA94
page(s)	376-382
instance of	wds:Q68127905-2994173A-E0F5-435B-8850-9121E0C2081D
instance of	scholarly article
PubMed ID	wds:Q68127905-D1B3B430-2EA5-4B6A-81D8-1B63EA1D5098
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1587801
PubMed ID	1587801
published in	wds:Q68127905-6629AA09-A41A-4E33-A54C-D04A1630E188
published in	Journal of Biochemistry
issue	wds:Q68127905-CC887C15-477E-410C-A295-8451BDA50749
volume	wds:Q68127905-774317D2-F562-49AF-9611-A5AC551EFCAF
issue	3
volume	111
number of pages	wds:Q68127905-2738CFD7-14B5-446B-A963-6E3B231767F6
number of pages	7 (xsd:decimal)
DOI	wds:Q68127905-66F8F561-35F9-43BF-BC38-91A2900E14FA
DOI	http://dx.doi.org/10.1093/OXFORDJOURNALS.JBCHEM.A123765
DOI	10.1093/OXFORDJOURNALS.JBCHEM.A123765
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68127905
is cites work of	Wavelength-dependent conformational changes in collagen after mid-infrared laser ablation of cornea Wavelength-dependent collagen fragmentation during mid-IR laser ablation Solid-state (13)C NMR reveals effects of temperature and hydration on elastin Crystallinity and compositional changes in carbonated apatites: Evidence from (31)P solid-state NMR, Raman, and AFM analysis High-resolution structural insights into bone: a solid-state NMR relaxation study utilizing paramagnetic doping. The mineral phase of calcified cartilage: its molecular structure and interface with the organic matrix Effects of tissue hydration on nanoscale structural morphology and mechanics of individual Type I collagen fibrils in the Brtl mouse model of Osteogenesis Imperfecta. Time-resolved dehydration-induced structural changes in an intact bovine cortical bone revealed by solid-state NMR spectroscopy. Solid-state NMR spectroscopy provides atomic-level insights into the dehydration of cartilage. Osmotic pressure induced tensile forces in tendon collagen. Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins New methods to study the composition and structure of the extracellular matrix in natural and bioengineered tissues 13C CPMAS NMR studies of the elastin‐like polypeptide (LGGVG)n 1H and 13C HR-MAS NMR investigations on native and enzymatically digested bovine nasal cartilage Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on [3-13C]Ala- and [1-13C]Val-labeled bacteriorhodopsin 13C NMR relaxation studies on cartilage and cartilage components Hydroxyproline Ring Pucker Causes Frustration of Helix Parameters in the Collagen Triple Helix Proline provides site-specific flexibility for in vivo collagen Total water, phosphorus relaxation and inter-atomic organic to inorganic interface are new determinants of trabecular bone integrity (13)C cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links. Selection of side-chain carbons in a high-molecular-weight, hydrophobic peptide using solid-state spectral editing methods. Conformation and dynamics of the [3-(13)C]Ala, [1-(13)C]Val-labeled truncated pharaonis transducer, pHtrII(1-159), as revealed by site-directed (13)C solid-state NMR: changes due to association with phoborhodopsin (sensory rhodopsin II) Pregnancy-Induced Dynamical and Structural Changes of Reproductive Tract Collagen
is cites work of	wds:Q31041571-91134115-8308-48EC-A54D-6A8AE66F0959 wds:Q37329758-9F6A1099-AA46-429E-A939-F4C525CE8862 wds:Q58177359-F4904013-F0B0-4B82-961C-C40174609097 wds:Q41085215-EF9B7862-1464-402A-905C-D81F6E5BC291 wds:Q47224471-99F9BB7C-F74A-4C41-B934-5F2467E3427A wds:Q54593365-4C65D545-332E-41FD-B1D6-5B533BC87EC3 wds:Q33515338-5022CCCA-D327-4F77-AFE8-B639D91D787A wds:Q30370971-1DE1638B-5AED-476F-BC95-43FE0B7881CD wds:Q34001644-FEB336E6-1199-42C5-97B6-5EF0B6705206 wds:Q33302483-B215CE31-4313-4C40-AB4A-243700A80A34 wds:Q42575577-A5924E93-038A-4E65-884C-0F357AC11EF7 wds:Q47596019-3B558176-6D0C-4242-86DA-B34ACAD995F1 wds:Q74319323-65AD5446-F4B4-40BE-8D1F-7857B413B6C2 wds:Q33970310-9DE0E6B8-7622-4B14-BCF8-EA34B18EB11E wds:Q30725567-D133F55F-D6A2-4B9B-B7B9-32CF733C5897 wds:Q30993212-B6F0E031-7D56-491D-98F9-98C7A12689A9 wds:Q34435371-B0867AE1-6922-40CF-8767-31D943009DD9 wds:Q37282292-346F69AB-4BC9-48D1-BB7F-D24D4D3CDA94 wds:Q30670811-4ED0259E-B43A-425E-9CFD-B22601054702 wds:Q36075900-E54B63AD-94D2-46E4-9A76-6D9926A5D887 wds:Q30603210-2F2BC93E-5E9E-42C6-97F7-241831CB3BB6 wds:Q57100990-42FBB773-9278-40D4-A274-7B5073B33D24 wds:Q34185701-0AE848E0-04ED-4E26-82AC-7DDBA1205D4F

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