Conformational changes in oxyhemoglobin c (Glu(beta 6)->lys) detected by spectroscopic probing

被引：25

作者：

Hirsch, RE

Lin, MJ

Vidugirus, GVA

Huang, SC

Friedman, JM

Nagel, RL

机构：

[1] YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT ANAT & STRUCT BIOL,BRONX,NY 10461

[2] YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT PHYSIOL & BIOPHYS,BRONX,NY 10461

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1996年 / 271卷 / 01期

关键词：

D O I：

10.1074/jbc.271.1.372

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：372 / 375

页数：4

共 24 条

[1]

ASHER SA, 1988, ANNU REV PHYS CHEM, V39, P537

[2]

Bunn HF., 1986, HEMOGLOBIN MOL GENET

[3]

Eaton W A, 1990, Adv Protein Chem, V40, P63, DOI 10.1016/S0065-3233(08)60287-9

[4] INTRAMOLECULAR ENERGY TRANSFER IN ADRENOCORTICOTROPIN [J].