THE ALPHA-HELICAL CONTENT OF CALMODULIN IS INCREASED BY SOLUTION CONDITIONS FAVORING PROTEIN CRYSTALLIZATION

被引:36
作者
BAYLEY, PM
MARTIN, SR
机构
[1] Division of Physical Biochemistry, National Institute for Medical Research, London, The Ridgeway
关键词
CALMODULIN; PROTEIN CRYSTALLIZATION; ALPHA-HELIX;
D O I
10.1016/0167-4838(92)90034-B
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
The conformation of porcine-brain calmodulin in solution has been examined by far-UV circular dichroism in the presence of 2-methyl 2,4-pentanediol, and polyethylene glycol which are used to promote the crystallisation of calmodulin. These organic compounds increase the alpha-helical content of Ca4-calmodulin to a significant degree and to a level similar to the alpha-helical content deduced from the crystal structure. These results support the view that in aqueous solution at pH 5-7, the conformation of Ca4-calmodulin is significantly different from the crystal structure and probably lacks at least a portion of the central helix. In the process of crystallisation, Ca4-calmodulin apparently adopts additional alpha-helical structure, probably due to the composition of the solution from which crystals are grown.
引用
收藏
页码:16 / 21
页数:6
相关论文
共 34 条
[1]   STRUCTURE OF CALMODULIN REFINED AT 2.2 A RESOLUTION [J].
BABU, YS ;
BUGG, CE ;
COOK, WJ .
JOURNAL OF MOLECULAR BIOLOGY, 1988, 204 (01) :191-204
[2]   3-DIMENSIONAL STRUCTURE OF CALMODULIN [J].
BABU, YS ;
SACK, JS ;
GREENHOUGH, TJ ;
BUGG, CE ;
MEANS, AR ;
COOK, WJ .
NATURE, 1985, 315 (6014) :37-40
[3]  
COOK WJ, 1983, METHOD ENZYMOL, V102, P143
[4]  
CRAIG TA, 1987, J BIOL CHEM, V262, P3278
[5]   EFFECT OF ALCOHOLS ON THE STRUCTURE OF CASEINS - CIRCULAR-DICHROISM STUDIES OF KAPPA-CASEIN-A [J].
GRIFFIN, MCA ;
PRICE, JC ;
MARTIN, SR .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 1986, 8 (06) :367-371
[6]   FREQUENCY-DOMAIN MEASUREMENTS OF THE ROTATIONAL-DYNAMICS OF THE TYROSINE GROUPS OF CALMODULIN [J].
GRYCZYNSKI, I ;
LAKOWICZ, JR ;
STEINER, RF .
BIOPHYSICAL CHEMISTRY, 1988, 30 (01) :49-59
[7]   INTENSITY AND ANISOTROPY DECAYS OF THE TYROSINE CALMODULIN PROTEOLYTIC FRAGMENTS, AS STUDIED BY GHZ FREQUENCY-DOMAIN FLUORESCENCE [J].
GRYCZYNSKI, I ;
STEINER, RF ;
LAKOWICZ, JR .
BIOPHYSICAL CHEMISTRY, 1991, 39 (01) :69-78
[8]   COMPARISON OF THE CRYSTAL AND SOLUTION STRUCTURES OF CALMODULIN AND TROPONIN-C [J].
HEIDORN, DB ;
TREWHELLA, J .
BIOCHEMISTRY, 1988, 27 (03) :909-915
[9]   CHANGES IN THE STRUCTURE OF CALMODULIN INDUCED BY A PEPTIDE BASED ON THE CALMODULIN-BINDING DOMAIN OF MYOSIN LIGHT CHAIN KINASE [J].
HEIDORN, DB ;
SEEGER, PA ;
ROKOP, SE ;
BLUMENTHAL, DK ;
MEANS, AR ;
CRESPI, H ;
TREWHELLA, J .
BIOCHEMISTRY, 1989, 28 (16) :6757-6764
[10]   TRIPLE-RESONANCE MULTIDIMENSIONAL NMR-STUDY OF CALMODULIN COMPLEXED WITH THE BINDING DOMAIN OF SKELETAL-MUSCLE MYOSIN LIGHT-CHAIN KINASE - INDICATION OF A CONFORMATIONAL CHANGE IN THE CENTRAL HELIX [J].
IKURA, M ;
KAY, LE ;
KRINKS, M ;
BAX, A .
BIOCHEMISTRY, 1991, 30 (22) :5498-5504