pubmed-article:9827996 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C0025852 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C0033095 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C0681842 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C0596957 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:9827996 | lifeskim:mentions | umls-concept:C1337528 | lld:lifeskim |
pubmed-article:9827996 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:9827996 | pubmed:dateCreated | 1999-1-21 | lld:pubmed |
pubmed-article:9827996 | pubmed:abstractText | We investigated the pathway for pressure unfolding of metmyoglobin using molecular dynamics (MD) for a range of pressures (0.1 MPa to 1.2 GPa) and a temperature of 300 K. We find that the unfolding of metmyoglobin proceeds via a two-step mechanism native --> molten globule intermediate --> unfolded, where the molten globule forms at 700 MPa. The simulation describes qualitatively the experimental behavior of metmyoglobin under pressure. We find that unfolding of the alpha-helices follows the sequence of migrating hydrogen bonds (i,i + 4) --> (i,i + 2). | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:language | eng | lld:pubmed |
pubmed-article:9827996 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9827996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9827996 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9827996 | pubmed:month | Nov | lld:pubmed |
pubmed-article:9827996 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:9827996 | pubmed:author | pubmed-author:GoddardW... | lld:pubmed |
pubmed-article:9827996 | pubmed:author | pubmed-author:DomontG BGB | lld:pubmed |
pubmed-article:9827996 | pubmed:author | pubmed-author:NascimentoM... | lld:pubmed |
pubmed-article:9827996 | pubmed:author | pubmed-author:FlorianoW BWB | lld:pubmed |
pubmed-article:9827996 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9827996 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:9827996 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9827996 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9827996 | pubmed:pagination | 2301-13 | lld:pubmed |
pubmed-article:9827996 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:meshHeading | pubmed-meshheading:9827996-... | lld:pubmed |
pubmed-article:9827996 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9827996 | pubmed:articleTitle | Effects of pressure on the structure of metmyoglobin: molecular dynamics predictions for pressure unfolding through a molten globule intermediate. | lld:pubmed |
pubmed-article:9827996 | pubmed:affiliation | Materials and Process Simulation Center, Beckman Institute, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA. | lld:pubmed |
pubmed-article:9827996 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9827996 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:9827996 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9827996 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9827996 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9827996 | lld:pubmed |