Conformational changes in oxyhemoglobin C (Glu beta 6-->Lys) detected by spectroscopic probing.
| Autoři: | Hirsch RE; Department of Medicine, Montefiore Medical Center, Bronx, New York, USA., Lin MJ, Vidugiris GJ, Huang S, Friedman JM, Nagel RL |
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| Zdroj: | The Journal of biological chemistry [J Biol Chem] 1996 Jan 05; Vol. 271 (1), pp. 372-5. |
| Způsob vydávání: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
| Jazyk: | English |
| Informace o časopise: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| Imprint Name(s): | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| Výrazy ze slovníku MeSH: | Glutamic Acid/*chemistry , Lysine/*chemistry , Oxyhemoglobins/*chemistry, Humans ; Protein Conformation ; Spectrum Analysis |
| Abstrakt: | Hemoglobin C (Glu beta 6-->Lys) shares with hemoglobin S (Glu beta 6-->Val) the site of mutation, but with different consequences: deoxyHbS forms polymers, whereas oxyHbC readily forms crystals. The molecular mechanism for this property of oxyHbC is unknown. Since no detailed oxyHbC crystal structural information exists, spectroscopic probing is used in this study to investigate possible solution-phase conformational changes in HbC compared with HbA. Intrinsic fluorescence combined with UV resonance Raman data demonstrate a weakening of the Trp beta 15-Ser beta 72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix. |
| Komentáře: | Erratum in: J Biol Chem 1998 Jul 17;273(29):18676. Vidugirus GV [corrected to Vidugiris GJ]. |
| Grant Information: | DK-41253 United States DK NIDDK NIH HHS; HL-38655 United States HL NHLBI NIH HHS; P01-HL-51084 United States HL NHLBI NIH HHS; etc. |
| Substance Nomenclature: | 0 (Oxyhemoglobins) 3KX376GY7L (Glutamic Acid) K3Z4F929H6 (Lysine) |
| Entry Date(s): | Date Created: 19960105 Date Completed: 19960220 Latest Revision: 20210210 |
| Update Code: | 20221213 |
| DOI: | 10.1074/jbc.271.1.372 |
| PMID: | 8550589 |
| Autor: | Hirsch RE; Department of Medicine, Montefiore Medical Center, Bronx, New York, USA., Lin MJ, Vidugiris GJ, Huang S, Friedman JM, Nagel RL |
| Jazyk: | angličtina |
| Zdroj: | The Journal of biological chemistry [J Biol Chem] 1996 Jan 05; Vol. 271 (1), pp. 372-5. |
| DOI: | 10.1074/jbc.271.1.372 |
| Abstrakt: | Hemoglobin C (Glu beta 6-->Lys) shares with hemoglobin S (Glu beta 6-->Val) the site of mutation, but with different consequences: deoxyHbS forms polymers, whereas oxyHbC readily forms crystals. The molecular mechanism for this property of oxyHbC is unknown. Since no detailed oxyHbC crystal structural information exists, spectroscopic probing is used in this study to investigate possible solution-phase conformational changes in HbC compared with HbA. Intrinsic fluorescence combined with UV resonance Raman data demonstrate a weakening of the Trp beta 15-Ser beta 72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix. |
| Databáze: | MEDLINE |
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