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Protein Folding. David Shiuan Department of Life Science, Institute of Biotechnology and Interdisciplinary Program of Bioinformatics National Dong Hwa University. Molecular Forces. Covalent Interaction Nonbonded Interaction
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Protein Folding David Shiuan Department of Life Science, Institute of Biotechnology and Interdisciplinary Program of Bioinformatics National Dong Hwa University
Molecular Forces • Covalent Interaction • Nonbonded Interaction - Electrostatic Interaction - Hydrophobic Interaction - Van der wall Force
PROTEIN FOLDING AND DISEASE • What happens if proteins don't fold correctly? Diseases such as Alzheimer's disease, cystic fibrosis, BSE (Mad Cow disease), an inherited form of emphysema, and even many cancers are believed to result from protein misfolding. • When proteins misfold, they can clump together ("aggregate"). These clumps can often gather in the brain, where they are believed to cause the symptoms of Mad Cow or Alzheimer's disease.
PROTEIN FOLDING AND NANOTECHNOLOGY Building man made machines on the nanoscale • In addition to biomedical applications, learning about how proteins fold will also teach us how to design our own protein-sized "nanomachines" to do similar tasks. Of course, before nanomachines can carry out any activity, they must also be assembled.
Structure Determination • 1. X-ray Diffraction • 2. NMR Spectroscopy • 3. Theoretical Calculation
Protein Structure • Primary Structure • Secondary Structure • Tertiary Structure • Quaternary Structure
Types of Secondary Structure • Helices • Sheets • Turns • Others
Types of Protein • Globular Protein • Membrane Protein • Fibrous and Structural Protein
Globular Protein • Most protein • Proteins > 200 aa have multi-domains
Protein Interactions • 1. Regulatory Protein and DNA • 2. Enzymes • 3. Allostery – hemoglobin • 4. Muscle Fibres
Insulin hexamer - zinc ions and 3 water coordinate with each