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Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchange
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Published in: | FEBS letters 1977-05, Vol.77 (1), p.103-106 |
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container_end_page | 106 |
container_issue | 1 |
container_start_page | 103 |
container_title | FEBS letters |
container_volume | 77 |
creator | Abaturov, L.V. Jinoria, K.Sh Varshavsky, Ya.M. Yakobashvily, N.N. |
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doi_str_mv | 10.1016/0014-5793(77)80202-0 |
format | article |
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Jinoria, K.Sh ; Varshavsky, Ya.M. ; Yakobashvily, N.N.</creator><creatorcontrib>Abaturov, L.V. ; Jinoria, K.Sh ; Varshavsky, Ya.M. ; Yakobashvily, N.N.</creatorcontrib><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(77)80202-0</identifier><identifier>PMID: 858384</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>deoxy Hb ; different ligand states of ferrihemoglobin A (MetHb) ; different ligand states of ferrohemoglobin A ; Drug Stability ; HbO2 and HbCO ; Heme ; hemoglobin A ; Hemoglobins ; Humans ; Kinetics ; Ligands ; MetHbH2O, MetHbOH and MetHbCN ; Methemoglobin ; Oxyhemoglobins ; Protein Binding ; Protein Conformation ; unliganded ferrohemoglobin A</subject><ispartof>FEBS letters, 1977-05, Vol.77 (1), p.103-106</ispartof><rights>1977</rights><rights>FEBS Letters 77 (1977) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4650-82e37b37679c0822f98185de6d1377d3e5fc004c6a858f9e0508b045b2452d8a3</citedby><cites>FETCH-LOGICAL-c4650-82e37b37679c0822f98185de6d1377d3e5fc004c6a858f9e0508b045b2452d8a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0014579377802020$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/858384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abaturov, L.V.</creatorcontrib><creatorcontrib>Jinoria, K.Sh</creatorcontrib><creatorcontrib>Varshavsky, Ya.M.</creatorcontrib><creatorcontrib>Yakobashvily, N.N.</creatorcontrib><title>Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchange</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><subject>deoxy Hb</subject><subject>different ligand states of ferrihemoglobin A (MetHb)</subject><subject>different ligand states of ferrohemoglobin A</subject><subject>Drug Stability</subject><subject>HbO2 and HbCO</subject><subject>Heme</subject><subject>hemoglobin A</subject><subject>Hemoglobins</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Ligands</subject><subject>MetHbH2O, MetHbOH and MetHbCN</subject><subject>Methemoglobin</subject><subject>Oxyhemoglobins</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>unliganded ferrohemoglobin A</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><recordid>eNqNkc1u3CAUhVHVv2naN8iCVZUs3IKxDd5UaqOZtlKkbto1wnCZocKQgietHyLvHDyOsuii6gIh7jn3A85F6JySd5TQ7j0htKla3rMLzi8FqUldkSdoQwVnFWs68RRtHi0v0aucf5JyFrR_gZ6LVjDRbNDd1lrQE44We7dXweBlHWAEHAPWMdiYRjW5GJTHeVKD826a8YULU1Jj9KCPXqW_jWOcTr7LhVtgce_j4AJWGSe4BeXB4GHGh9mkuIeA4Y8-qLCH1-iZVT7Dm4f9DP3Ybb9ffamuv33-evXxutJN15JK1MD4wHjHe01EXdteUNEa6AxlnBsGrdWENLpT5Zu2B9ISMZCmHeqmrY1Q7Ay9Xbk3Kf46Qp7k6LIG71WAeMyyZCMaymkxNqtRp5hzAitvkhtVmiUlchmCXBKWS8KSc3kagiSl7fyBfxxGMI9Na-pF3q3yb-dh_i-k3G0_1Yuw1Dk_VZd7PqwgKGHdOkgyawdBg3GpTFWa6P790HtQXKsx</recordid><startdate>19770501</startdate><enddate>19770501</enddate><creator>Abaturov, L.V.</creator><creator>Jinoria, K.Sh</creator><creator>Varshavsky, Ya.M.</creator><creator>Yakobashvily, N.N.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19770501</creationdate><title>Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchange</title><author>Abaturov, L.V. ; 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identifier | ISSN: 0014-5793 |
ispartof | FEBS letters, 1977-05, Vol.77 (1), p.103-106 |
issn | 0014-5793 1873-3468 |
language | eng |
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source | ScienceDirect® |
subjects | deoxy Hb different ligand states of ferrihemoglobin A (MetHb) different ligand states of ferrohemoglobin A Drug Stability HbO2 and HbCO Heme hemoglobin A Hemoglobins Humans Kinetics Ligands MetHbH2O, MetHbOH and MetHbCN Methemoglobin Oxyhemoglobins Protein Binding Protein Conformation unliganded ferrohemoglobin A |
title | Effect of ligand and heme on conformational stability (intramolecular conformational motility) of hemoglobin as revealed by hydrogen exchange |
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