Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II

被引:27
作者
Jonasson, P
Aronsson, G
Carlsson, U
Jonsson, BH
机构
[1] UMEA UNIV,DEPT BIOCHEM,S-90187 UMEA,SWEDEN
[2] LINKOPING UNIV,IFM,DEPT CHEM,S-58183 LINKOPING,SWEDEN
关键词
D O I
10.1021/bi961882a
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 refolding reaction of human carbonic anhydrase II has been characterized by use of seven variants in which tryptophan residues have been replaced by Phe or Cys, in each case giving proteins with six tryptophans. Intrinsic tryptophan fluorescence was used to monitor the refolding in the 2 ms-60 s time range, and kinetic traces showing the contributions from each particular tryptophan were obtained by calculation of differences between the wild-type protein and the variants. Earlier assignment [Martensson, L.-G., Jonasson, P., Freskgard, P.-O., Svensson, M., Carlsson, U., & Jonsson, B.-H. (1995) Biochemistry, 34, 1011-1021] of specific fluorescence properties to each tryptophan, especially regarding energy transfer and intrinsic fluorescence quenching, has made it possible to use the kinetic data to describe the formation of tertiary structure at defined tryptophan residues. In summary, it was found that tertiary structure is formed earlier at those tryptophans that are associated with the central core of beta-strands than at tryptophan residues in the N-terminal minidomain.
引用
收藏
页码:5142 / 5148
页数:7
相关论文
共 16 条
[1]   FOLDING AND STABILITY OF THE N-TERMINUS OF HUMAN CARBONIC-ANHYDRASE-II [J].
ARONSSON, G ;
MARTENSSON, LG ;
CARLSSON, U ;
JONSSON, BH .
BIOCHEMISTRY, 1995, 34 (07) :2153-2162
[2]   THE ROLE OF THE METAL-ION IN THE REFOLDING OF DENATURED BOVINE CO(II)-CARBONIC ANHYDRASE-II [J].
BERGENHEM, N ;
CARLSSON, U .
BIOCHIMICA ET BIOPHYSICA ACTA, 1989, 998 (03) :277-285
[3]   REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE-II AT 2.0-A RESOLUTION [J].
ERIKSSON, AE ;
JONES, TA ;
LILJAS, A .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1988, 4 (04) :274-282
[4]   CIS-TRANS ISOMERIZATION IS RATE-DETERMINING IN THE REACTIVATION OF DENATURED HUMAN CARBONIC ANHYDRASE-II AS EVIDENCED BY PROLINE ISOMERASE [J].
FRANSSON, C ;
FRESKGARD, PO ;
HERBERTSSON, H ;
JOHANSSON, A ;
JONASSON, P ;
MARTENSSON, LG ;
SVENSSON, M ;
JONSSON, BH ;
CARLSSON, U .
FEBS LETTERS, 1992, 296 (01) :90-94
[5]   ASSIGNMENT OF THE CONTRIBUTION OF THE TRYPTOPHAN RESIDUES TO THE CIRCULAR-DICHROISM SPECTRUM OF HUMAN CARBONIC-ANHYDRASE .2. [J].
FRESKGARD, PO ;
MARTENSSON, LG ;
JONASSON, P ;
JONSSON, BH ;
CARLSSON, U .
BIOCHEMISTRY, 1994, 33 (47) :14281-14288
[6]   STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE-II AND STRUCTURE OF SOME OF ITS ANION LIGAND COMPLEXES [J].
HAKANSSON, K ;
CARLSSON, M ;
SVENSSON, LA ;
LILJAS, A .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 227 (04) :1192-1204
[7]   REACTIVATION KINETICS OF GUANIDINE DENATURED BOVINE CARBONIC ANHYDRASE-B [J].
IKAI, A ;
TANAKA, S ;
NODA, H .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1978, 190 (01) :39-45
[8]   MOLSCRIPT - A PROGRAM TO PRODUCE BOTH DETAILED AND SCHEMATIC PLOTS OF PROTEIN STRUCTURES [J].
KRAULIS, PJ .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1991, 24 :946-950
[9]   INHIBITION AND CATALYSIS OF CARBONIC-ANHYDRASE - RECENT CRYSTALLOGRAPHIC ANALYSES [J].
LILJAS, A ;
HAKANSSON, K ;
JONSSON, BH ;
XUE, YF .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1994, 219 (1-2) :1-10
[10]   CHARACTERIZATION OF FOLDING INTERMEDIATES OF HUMAN CARBONIC-ANHYDRASE .2. PROBING SUBSTRUCTURE BY CHEMICAL LABELING OF SH-GROUPS INTRODUCED BY SITE-DIRECTED MUTAGENESIS [J].
MARTENSSON, LG ;
JONSSON, BH ;
FRESKGARD, PO ;
KIHLGREN, A ;
SVENSSON, M ;
CARLSSON, U .
BIOCHEMISTRY, 1993, 32 (01) :224-231