Protein folding

A. Szilágyi, J. Kardos, S. Osváth, L. Barna, P. Závodszky

Research output: Chapter

12 Citations (Scopus)


Since Anfinsen's famous experiments in the 1960s, it has been known that the complex three-dimensional structure of protein molecules is encoded in their amino acid sequences, and the chains autonomously fold under proper conditions. Cracking this code, which is sometimes called the second part of the genetic code, has been one of the greatest challenges of molecular biology. Although a full understanding of how proteins fold remains elusive, theoretical and experimental studies of protein folding have come a long way since Anfinsen's findings. In the living cell, folding occurs in a complex and crowded environment, often involving helper proteins, and in some cases it can go awry: the protein can misfold, aggregate, or form amyloid fibers. It is increasingly recognized that misfolded proteins and amyloid formation are the root cause of a number of serious illnesses including several neurodegenerative diseases. Therefore, the study of protein folding remains a key area of biomedical research.

Original languageEnglish
Title of host publicationHandbook of Neurochemistry and Molecular Neurobiology
Subtitle of host publicationNeural Protein Metabolism and Function
PublisherSpringer US
Number of pages41
ISBN (Print)9780387303468
Publication statusPublished - dec. 1 2007


ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Szilágyi, A., Kardos, J., Osváth, S., Barna, L., & Závodszky, P. (2007). Protein folding. In Handbook of Neurochemistry and Molecular Neurobiology: Neural Protein Metabolism and Function (pp. 303-343). Springer US.