Sequence-based study of two related proteins with different folding behaviors

被引：2

作者：

Favrin, G ^{[1
]}

Irbäck, A ^{[1
]}

Wallin, S ^{[1
]}

机构：

[1] Lund Univ, Dept Theoret Phys, Complex Syst Div, SE-22362 Lund, Sweden

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2004年 / 54卷 / 01期

关键词：

protein folding; folding thermodynamics; folding kinetics; three-helix bundle; unstructured protein; Monte Carlo simulation;

D O I：

10.1002/prot.10575

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：

Z(SPA-1) is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed Z(SPA-1) shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction. (C) 2003 Wiley-Liss, Inc.

引用

页码：8 / 12

页数：5

共 12 条

[1] Folding pathways of proteins with increasing degree of sequence identities but different structure and function
Giri, Rajanish
Morrone, Angela
Travaglini-Allocatelli, Carlo
Jemth, Per
Brunori, Maurizio
Gianni, Stefano
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (44) : 17772 - 17776
[2] Different circular permutations produced different folding nuclei in proteins: A computational study
Li, L
Shakhnovich, EI
JOURNAL OF MOLECULAR BIOLOGY, 2001, 306 (01) : 121 - 132
[3] Exploring the conformational properties of the sequence space between two proteins with different folds: An experimental study
Blanco, FJ
Angrand, I
Serrano, L
JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (02) : 741 - 753
[4] Conserved structural topologies in RNase A-like and trypsin-like serine proteases: a sequence-based folding analysis
K. M. Ahsanul Kabir
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BMC Molecular and Cell Biology, 26 (1)
[5] Amino acid sequence predicts folding rate for middle-size two-state proteins
Huang, JT
Tian, J
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2006, 63 (03) : 551 - 554
[6] Comparison of the transition states for folding of two Ig-like proteins from different superfamilies
Geierhaas, CD
Paci, E
Vendruscolo, M
Clarke, J
JOURNAL OF MOLECULAR BIOLOGY, 2004, 343 (04) : 1111 - 1123
[7] Folding kinetics of two-state proteins based on the model of general random walk in native contact number space
Guo, J. S.
Mi, D.
Sun, Y. Q.
PHYSICA A-STATISTICAL MECHANICS AND ITS APPLICATIONS, 2010, 389 (04) : 761 - 766
[8] Sequence and structural analysis of two designed proteins with 88% identity adopting different folds
Mani, Saravanan K.
Balasubramanian, Harihar
Nallusamy, Saranya
Samuel, Selvaraj
PROTEIN ENGINEERING DESIGN & SELECTION, 2010, 23 (12) : 911 - 918
[9] Accurate prediction of the folding rate for two-state proteins based on amino acid sequences
Zhao, Chunyan
Zhu, Yu
Zhang, Haixia
Liu, Mancang
Fan, Botao
QSAR & COMBINATORIAL SCIENCE, 2007, 26 (03): : 307 - 316
[10] A Hamiltonian Replica Exchange Molecular Dynamics (MD) Method for the Study of Folding, Based on the Analysis of the Stabilization Determinants of Proteins
Meli, Massimiliano
Colombo, Giorgio
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2013, 14 (06): : 12157 - 12169

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