Principles that govern the folding of protein chains.

@article{Anfinsen1973PrinciplesTG,
  title={Principles that govern the folding of protein chains.},
  author={Christian B. Anfinsen},
  journal={Science},
  year={1973},
  volume={181 4096},
  pages={
          223-30
        }
}
  • C. Anfinsen
  • Published 20 July 1973
  • Chemistry, Medicine
  • Science
Stanford Moore, William Stein, and Anfinsen were awarded the Nobel Prize in Chemistry in 1972 for "their contribution to the understanding of the connection between chemical structure and catalytic activity of the active center of the ribonuclease molecule." In his Nobel Lecture, Anfinsen provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the "Thermodynamic Hypothesis," and outlined potential avenues of current and future… 
Protein folding and unfolding.
  • F. Pohl
  • Chemistry, Medicine
    Molecular biology, biochemistry, and biophysics
  • 1977
TLDR
The elucidation of the pathways of folding, the magnitude of the different thermodynamic forces involed, and the kinetics of such processes are still in a relatively early stage of investigation.
Genetic Analysis of Polypeptide Chain Folding and Misfolding in Vivo
Some 30 years have passed since the first protein structures were determined by X-ray crystallography, and since Anfinsen and co-workers established that the information for determining conformation
The Development of the Prediction of Protein Structure
The tenet of structural biology that function follows form had its seeds in the monograph by C. B. Anfinsen, The Molecular Basis of Evolution (Anfinsen, 1959), wherein he stated “Protein chemists
The Physics of the Interactions Governing Folding and Association of Proteins
Abstract: The review discusses the molecular origins of the forces and free energies that determine several things about proteins, and how experiment and theory reveal this information. The first
Theoretical studies of protein-folding thermodynamics and kinetics.
  • E. Shakhnovich
  • Chemistry, Medicine
    Current opinion in structural biology
  • 1997
TLDR
Recently, protein-folding models have advanced to the point where folding simulations of protein-like chains of reasonable length are feasible, and the major physical features of folding proteins can be reproduced, allowing deep insight into the physical mechanism of folding.
Is stoichiometry a new metric for evaluating folded proteins?
TLDR
These results suggested that non-bonded interactions drive protein folding rather than the random pairing of stronger covalent disulfide bridges.
A surprising simplicity to protein folding
TLDR
The fundamental physics underlying folding may be much simpler than this complexity would lead us to expect: folding rates and mechanisms appear to be largely determined by the topology of the native (folded) state.
Protein folding: concepts and perspectives
  • J. Yon
  • Chemistry, Medicine
    Cellular and Molecular Life Sciences CMLS
  • 1997
TLDR
It can be concluded that the main rules deduced from the in vitro folding studies are valid for the folding of a nascent polypeptide chain in vivo.
Adding backbone to protein folding: why proteins are polypeptides.
TLDR
It is argued that the chemical nature of the polypeptide backbone is the central determinant of the three-dimensional structures of proteins and 'Sidechain-only' models, based on hydrophobicity patterns, fail to account for the properties of the backbone and thus will have difficulty capturing essential features of a folding pathway.
Mutations and the conformational stability of globular proteins
TLDR
The results of such studies on stability variants of human haemoglobin and of T4 phage lysozyme are described.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 52 REFERENCES
SOME RELATIONSHIPS OF STRUCTURE TO FUNCTION IN RIBONUCLEASE
This study by White and Anfinsen on the renaturation of fully denatured ribonuclease, or RNase, required subsequent supporting investigations to establish what came to be called the "thermodynamic
Reductive cleavage of disulfide bridges in ribonuclease.
This article was the first of many studies that were generally concerned with the eventual total synthesis of the protein. It contained several original observations that would lead to the
Studies on the mechanism of the enzymic catalysis of disulfide interchange in proteins.
TLDR
An enzyme that catalyzes disulfide interchange in proteins, localized in the microsomes of all tissues tested, has been isolated in pure form from bovine liver microsome and appears to be essential for enzymic activity.
The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain.
TLDR
There existed a considerable lag phase before enzymatic activity appeared after the sample of bovine pancreatic ribonuclease was treated with mercaptoethanol in urea, during which period the sulfhydrl titer and the specific optical rotation changed along a curve similar to that of a first-order reaction.
The sequence of the amino acid residues in performic acid-oxidized ribonuclease.
TLDR
The present communication reports the results of sequence studies on each of the peptides, studies which have led to the proposed complete formula for oxidized ribonuclease given in Fig. 1.
Nuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments.
TLDR
This is one of many articles produced by Anfinsen's research team and others on the factors contributing to the translation of the genetic message for a particular protein backbone and found that some proteins could be cleaved into two, or even three, fragments that recombined through non-covalent forces to yield biologically active structures with physical properties very similar to those of the parent protein molecules.
The synthesis of ribonuclease A.
TLDR
A protected linear polypeptide of 124 amino acid residues with the sequence of bovine pancreatic ribonuclease A was synthesized by the solid phase method, showing the high substrate specificity to be expected of RNase A and indicating that the five NH2-terminal residues of S-protein are not required for the protein to oxidize and fold in the presence of s-peptides to give an active enzyme.
Side-chain interactions governing the pairing of half-cystine residues in ribonuclease.
TLDR
The observation that this mixture of materials can be readily converted to the native structure is taken as evidence that the unique secondary and tertiary structure of RNase is, thermodynamically, the most stable configuration.
Folding of staphylococcal nuclease: magnetic resonance and fluorescence studies of individual residues.
TLDR
Findings indicate that local conformational changes can be detected by magnetic resonance spectroscopy in the cooperative transition of the overall structure.
Purification of synthetic ribonuclease S-peptide derivatives by specific complex formation on columns of ribonuclease S-protein bound to agarose.
TLDR
The chemical and catalytic properties of the purified materials suggest the presence of closely related side products, formed during the synthesis or during subsequent deprotection steps which bind tightly to the S-protein conjugate but which yield enzymically inactive complexes with RNase S- protein.
...
1
2
3
4
5
...