Dominant forces in protein folding.
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Summary
The present review aims to provide a reassessment of the factors important for folding in light of current knowledge, including contributions to the free energy of folding arising from electrostatics, hydrogen-bonding and van der Waals interactions, intrinsic propensities, and hydrophobic interactions.
- Type
- review
- Published
- 1990-08-07
- Cited by
- 3,539
- References
- 285
- OpenAlex
- https://openalex.org/W2070783701
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:30690389
Keywords
Citation, Altmetrics, Icon, Social media, Computer science
References
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- Principles of polymer chemistry
- Analysis of sequence-similar pentapeptides in unrelated protein tertiary structures. Strategies for protein folding and a guide for site-directed mutagenesis.
- An analysis of incorrectly folded protein models. Implications for structure predictions.
- Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix.
- Weakly polar interactions in proteins.
- Partial Molal Volumes of Hydrocarbons in Water Solution
- Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn.
Cited by
- An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
- Proper and improper folding of proteins in the cellular environment.
- Computational and experimental studies of protein kinase-inhibitor interactions
- Differential scanning calorimetry of proteins.
- The Hydrophobic Nature of GroEL-Substrate Binding (*)
- Thermodynamics of unfolding of the all beta-sheet protein interleukin-1 beta.
- Structural and thermodynamic aspects of the hydrophobic effect.
- Protein Secondary Structure Prediction
- Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins.
- Serine proteinases from cold-adapted organisms.
- Identification of disulphide bonds in the refolding of bovine pancreatic RNase A.
- Consistency in structural energetics of protein folding and peptide recognition
- A magnesium ion core at the heart of a ribozyme domain
- Emerging themes in RNA folding.
- Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy.
- Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme.
- Heat capacity of hydrogen-bonded networks: an alternative view of protein folding thermodynamics.
- Practical Approaches to Protein Folding and Assembly
- Helicogenicity of solvents in the conformational equilibrium of oligo(m-phenylene ethynylene)s: Implications for foldamer research
- Detection of an Intermediate during Unfolding of Bacterial Cell Division Protein FtsZ
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