Allosteric Transition Intermediates Modeled By Cross-linked Hemoglobins
dc.contributor.author | Schumacher, M. A. | en_US |
dc.contributor.author | Dixon, M. M. | en_US |
dc.contributor.author | Kluger, R. | en_US |
dc.contributor.author | Jones, Richard T. | en_US |
dc.contributor.author | Brennan, R. G. | en_US |
dc.date.accessioned | 2009-06-01T17:32:55Z | |
dc.date.available | 2009-06-01T17:32:55Z | |
dc.date.issued | 1995-05-04 | en_US |
dc.identifier.citation | Schumacher, MA; Dixon, MM; Kluger, R; Jones, RT; Brennan, RG. (1995) "Allosteric Transition Intermediates Modeled By Cross-linked Hemoglobins." Nature 375(6526): 84-87. <http://hdl.handle.net/2027.42/62708> | en_US |
dc.identifier.issn | 0028-0836 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/62708 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7723849&dopt=citation | en_US |
dc.description.abstract | THE structural end-points of haemoglobin's transition from its low-oxygen-affinity (T) to high-oxygen-affinity CR) state, have been well established by X-ray crystallography(1-7), but short-lived intermediates have proved less amenable to X-ray studies, Here we use chemical crosslinking to fix these intermediates for structural characterization. We describe the X-ray structures of three haemoglobins, alpha(2) beta(1)S(82)beta, alpha(2) beta(1)Tm(82)beta and alpha(2) beta(1,82)Tm(82)beta, which were crosslinked between the amino groups of residues beta Val1 and beta Lys82 by 3,3'-stilbenedicarboxylic acid (S) or trimesic acid (Tm) while in the deoxy state, and saturated with carbon monoxide before crystallization. alpha(2) beta(1)S(82)beta, which has almost normal oxygen affinity, is completely in the R-state conformation; however, alpha(2) beta(1)Tm(82)beta and alpha(2) beta(1,82)Tm(82)beta, both of which have low oxygen affinity, have been prevented from completing their transition into the R state and display many features of a transitional intermediate, These haemoglobins therefore represent a snapshot of the nascent R state. | en_US |
dc.format.extent | 658057 bytes | |
dc.format.extent | 2489 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Macmillan Magazines Ltd. | en_US |
dc.source | Nature | en_US |
dc.title | Allosteric Transition Intermediates Modeled By Cross-linked Hemoglobins | en_US |
dc.type | Article | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | UNIV MICHIGAN,DIV BIOPHYS RES,ANN ARBOR,MI 48109 | en_US |
dc.contributor.affiliationother | UNIV TORONTO,DEPT CHEM,LASH MILLER LABS,TORONTO,ON M5S 1A1,CANADA | en_US |
dc.identifier.pmid | 7723849 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/62708/1/375084a0.pdf | |
dc.identifier.doi | http://dx.doi.org/10.1038/375084a0 | en_US |
dc.identifier.source | Nature | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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