Identification and Characterization of Molten Globule-Like State of Hen Egg-White Lysozyme in Presence of Salts Under Alkaline Conditions

被引:19
作者
Ansari, M. A. [1 ]
Zubair, S. [2 ]
Atif, S. M. [1 ]
Kashif, M. [1 ]
Khan, N. [1 ]
Rehan, M. [1 ]
Anwar, T. [1 ]
Iqbal, A. [3 ]
Owais, M. [1 ]
机构
[1] Aligarh Muslim Univ, Interdisciplinary Biotechnol Unit, Aligarh 202002, Uttar Pradesh, India
[2] Aligarh Muslim Univ, Womens Coll, Aligarh 202002, Uttar Pradesh, India
[3] Aligarh Muslim Univ, Dept Agr Microbiol, Aligarh 202002, Uttar Pradesh, India
关键词
Lysozyme; secondary structure; molten globule; ELECTROSTATIC INTERACTIONS; INTERMEDIATE STATE; STRUCTURAL-CHARACTERIZATION; CIRCULAR-DICHROISM; ALPHA-LACTALBUMIN; PROTEIN-STRUCTURE; ESCHERICHIA-COLI; CYTOCHROME-C; BINDING; COOPERATIVITY;
D O I
10.2174/092986610789909502
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
In the present study, we elucidated the effect of potassium salts on alkali denatured hen egg white lysozyme (EC 3.2.1.17) using intrinsic/extrinsic fluorescence as well circular dichroism (CD) spectroscopic methods. Intrinsic fluorescence studies revealed that various potassium salts mediate stabilization of lysozyme against alkali denaturation. Far and near UV CD spectrum studies, showed that 2M KCl induced appreciable amount of secondary structure with minimum tertiary contacts in lysozyme at pH 12.6. Acrylamide quenching studies suggest that at pH 12.6, the presence of 2M KCl causes reduced accessibility of the quencher to tryptophan residues of the protein presumably because of its compact conformation. In summary, the results of present study suggest that lysozyme attains a compact folded intermediate with molten globule like characteristics at alkaline pH in presence of potassium chloride.
引用
收藏
页码:11 / 17
页数:7
相关论文
共 58 条
[1]   8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions [J].
Ali, V ;
Prakash, K ;
Kulkarni, S ;
Ahmad, A ;
Madhusudan, KP ;
Bhakuni, V .
BIOCHEMISTRY, 1999, 38 (41) :13635-13642
[2]  
Arai M, 2000, ADV PROTEIN CHEM, V53, P209
[3]   WHY PREFERENTIAL HYDRATION DOES NOT ALWAYS STABILIZE THE NATIVE STRUCTURE OF GLOBULAR-PROTEINS [J].
ARAKAWA, T ;
BHAT, R ;
TIMASHEFF, SN .
BIOCHEMISTRY, 1990, 29 (07) :1924-1931
[4]   PREFERENTIAL INTERACTIONS OF PROTEINS WITH SALTS IN CONCENTRATED-SOLUTIONS [J].
ARAKAWA, T ;
TIMASHEFF, SN .
BIOCHEMISTRY, 1982, 21 (25) :6545-6552
[5]   REFINEMENT OF HUMAN LYSOZYME AT 1.5 A RESOLUTION ANALYSIS OF NONBONDED AND HYDROGEN-BOND INTERACTIONS [J].
ARTYMIUK, PJ ;
BLAKE, CCF .
JOURNAL OF MOLECULAR BIOLOGY, 1981, 152 (04) :737-762
[6]  
BALDWIN RL, 1995, J BIOMOL NMR, V5, P103
[7]   A PARTIALLY FOLDED STATE OF HEN EGG-WHITE LYSOZYME IN TRIFLUOROETHANOL - STRUCTURAL CHARACTERIZATION AND IMPLICATIONS FOR PROTEIN FOLDING [J].
BUCK, M ;
RADFORD, SE ;
DOBSON, CM .
BIOCHEMISTRY, 1993, 32 (02) :669-678
[8]   KINETIC RESOLUTION OF PEPTIDE-BOND AND SIDE-CHAIN FAR-UV CIRCULAR-DICHROISM DURING THE FOLDING OF HEN EGG-WHITE LYSOZYME [J].
CHAFFOTTE, AF ;
GUILLOU, Y ;
GOLDBERG, ME .
BIOCHEMISTRY, 1992, 31 (40) :9694-9702
[9]   DETERMINATION OF SECONDARY STRUCTURES OF PROTEINS BY CIRCULAR-DICHROISM AND OPTICAL ROTATORY DISPERSION [J].
CHEN, YH ;
YANG, JT ;
MARTINEZ, HM .
BIOCHEMISTRY, 1972, 11 (22) :4120-+
[10]   THE HOFMEISTER EFFECT AND THE BEHAVIOR OF WATER AT INTERFACES [J].
COLLINS, KD ;
WASHABAUGH, MW .
QUARTERLY REVIEWS OF BIOPHYSICS, 1985, 18 (04) :323-422