Hydrophobic environment is a key factor for the stability of thermophilic proteins

Integrated prediction of protein folding and unfolding rates from only size and structural class

(2011) David De Sancho et al.   PHYSICAL CHEMISTRY CHEMICAL PHYSICS

Influence of long-range contacts and surrounding residues on the transition state structures of proteins

(2010) M. Michael Gromiha   ANALYTICAL BIOCHEMISTRY

Five mutations in N-terminus confer thermostability on mesophilic xylanase

(2010) Shan Zhang et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Comparative analysis of thermophilic and mesophilic proteins using Protein Energy Networks

(2010) MS Vijayabaskar et al.   BMC BIOINFORMATICS

Thermophilic enzymes and their applications in biocatalysis: a robust aldo‐keto reductase

(2010) Simon Willies et al.   ENVIRONMENTAL TECHNOLOGY

Enhanced Stability of a Protein with Increasing Temperature

(2010) Joachim M. Vinther et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Subunit interfaces of oligomeric hyperthermophilic enzymes display enhanced compactness

(2009) Fulvio Baldasseroni et al.   INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

Multiple Contact Network Is a Key Determinant to Protein Folding Rates

(2009) M. Michael Gromiha   Journal of Chemical Information and Modeling

Palaeotemperature trend for Precambrian life inferred from resurrected proteins

(2008) Eric A. Gaucher et al.   NATURE