Title

Investigation of protein unfolding and stability by computer simulation

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

1995-04-29

Document Type

Article

Subjects

Amino Acid Sequence; Animals; Cattle; Chickens; Computer Simulation; Molecular Sequence Data; Muramidase; Pancreatin; Plant Proteins; *Protein Folding; Protein Structure, Secondary; Repressor Proteins; Surface-Active Agents; Trypsin Inhibitors; Viral Proteins; alpha-Amylases

Disciplines

Amino Acids, Peptides, and Proteins | Biochemistry, Biophysics, and Structural Biology | Computer Sciences | Health Information Technology | Pharmacology, Toxicology and Environmental Health

Abstract

Structural, dynamic and energetic properties of proteins in solution can be studied in atomic detail by molecular dynamics computer simulation. Protein unfolding can be caused by a variety of driving forces induced in different ways: increased temperature or pressure, change of solvent composition, or protein amino acid mutation. The stability and unfolding of four different proteins (bovine pancreatic trypsin inhibitor, hen egg white lysozyme, the surfactant protein C and the DNA-binding domain of the 434 repressor) have been studied by applying the afore-mentioned driving forces and also to some artificial forces. The results give a picture of protein (in)stability and possible unfolding pathways, and are compared to experimental data where possible.

Keywords

Solvents, Simulations, Molecules, Protein unfolding, Dietary protein, Molecular dynamics, Biochemistry, Computer simulation

DOI of Published Version

10.1098/rstb.1995.0045

Source

Philos Trans R Soc Lond B Biol Sci. 1995 Apr 29;348(1323):49-59. Link to article on publisher's site

Journal/Book/Conference Title

Philosophical transactions of the Royal Society of London. Series B, Biological sciences

Related Resources

Link to Article in PubMed

PubMed ID

7770486

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