Elucidation of determinants of protein stability through genome sequence analysis

FEBS Letters

Chakravarty, Suvobrata¹  Varadarajan, Raghavan¹ 

[1] Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India

关键词: Genome;    Thermostability;    Secondary structure prediction;    t-Test;    fAg;    proportion of a particular residue in genome;    fr-h;    fraction of residues in helix;    fr-b;    fraction of residues in sheet;    fr-l;    fraction of residues in loops;    Sb3;    number of salt bridges of type i±3 per helix;    Sb4;    number of salt bridges of i±4 per helix;    dN;    net charge at N-terminus of helix;    dC;    net charge at C-terminus of helix;    Nc;    fraction of helices with N-capping boxes;    β-b;    number of β-branched residues per helix;    ORF;    open reading frame;    X T;    average value of a trait in thermophilic sample;    X M;    average value of a trait in mesophilic sample;   

DOI  :  10.1016/S0014-5793(00)01267-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sequences of putative soluble proteins from complete genomes of eight thermophiles and 12 mesophiles were analyzed to gain insight into determinants of protein thermostability. The predator algorithm was used to assign secondary structures to each protein sequence. Based on simple statistical tests, a set of stabilizing factors was identified. These include reduced protein size, increases in number of residues involved in hydrogen bonding, β-strand content and helix stabilization through ion pairs. There are also significant increases in the relative amounts of charged and hydrophobic β-branched amino acids and decreases in uncharged polar amino acids in proteins from thermophiles relative to mesophilic organisms. Factors such as the relative proportion of residues in loops, proline and glycine content and helix capping do not appear to be important.

【 授权许可】

Unknown