| pubmed-article:1599940 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1599940 | lifeskim:mentions | umls-concept:C0008746 | lld:lifeskim |
| pubmed-article:1599940 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:1599940 | lifeskim:mentions | umls-concept:C0260249 | lld:lifeskim |
| pubmed-article:1599940 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:1599940 | pubmed:dateCreated | 1992-7-14 | lld:pubmed |
| pubmed-article:1599940 | pubmed:abstractText | Changes in the secondary structure and aggregation of chymotrypsinogen were investigated by infrared difference spectroscopy in conjunction with temperature and pressure tuning IR spectroscopy; both the amide I' band and side chain bands were studied. A prominent component of the amide I' band in the difference spectrum obtained upon cooling a chymotrypsinogen solution, or increasing the hydrostatic pressure, was observed in the region between 1627 and 1622 cm-1. Under denaturing conditions a white gel was formed, which is attributed to irreversible self-association or aggregation. This process was accompanied by the appearance of two new amide I' bands in the infrared spectrum of the protein: a very strong band at 1618 cm-1 and a weak band at 1685 cm-1. These bands are assigned to peptide segments with anti-parallel aligned beta-strands. | lld:pubmed |
| pubmed-article:1599940 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1599940 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1599940 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1599940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1599940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1599940 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1599940 | pubmed:month | May | lld:pubmed |
| pubmed-article:1599940 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1599940 | pubmed:author | pubmed-author:MantschH HHH | lld:pubmed |
| pubmed-article:1599940 | pubmed:author | pubmed-author:IsmailA AAA | lld:pubmed |
| pubmed-article:1599940 | pubmed:author | pubmed-author:WongP TPT | lld:pubmed |
| pubmed-article:1599940 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1599940 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:1599940 | pubmed:volume | 1121 | lld:pubmed |
| pubmed-article:1599940 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1599940 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1599940 | pubmed:pagination | 183-8 | lld:pubmed |
| pubmed-article:1599940 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:1599940 | pubmed:meshHeading | pubmed-meshheading:1599940-... | lld:pubmed |
| pubmed-article:1599940 | pubmed:meshHeading | pubmed-meshheading:1599940-... | lld:pubmed |
| pubmed-article:1599940 | pubmed:meshHeading | pubmed-meshheading:1599940-... | lld:pubmed |
| pubmed-article:1599940 | pubmed:meshHeading | pubmed-meshheading:1599940-... | lld:pubmed |
| pubmed-article:1599940 | pubmed:meshHeading | pubmed-meshheading:1599940-... | lld:pubmed |
| pubmed-article:1599940 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1599940 | pubmed:articleTitle | Aggregation of chymotrypsinogen: portrait by infrared spectroscopy. | lld:pubmed |
| pubmed-article:1599940 | pubmed:affiliation | Steacie Institute for Molecular Sciences, National Research Council of Canada, Ottawa. | lld:pubmed |
| pubmed-article:1599940 | pubmed:publicationType | Journal Article | lld:pubmed |
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