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Journal ArticleDOI

Conformation Changes of Proteins

Rufus Lumry, +1 more
- 01 Feb 1954 - 
- Vol. 58, Iss: 2, pp 110-120
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This article is published in The Journal of Physical Chemistry.The article was published on 1954-02-01. It has received 824 citations till now.

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Journal ArticleDOI

Principles that Govern the Folding of Protein Chains

TL;DR: Anfinsen as discussed by the authors 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 scientific exploration.
Book ChapterDOI

Some factors in the interpretation of protein denaturation.

TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Journal ArticleDOI

Dominant forces in protein folding

TL;DR: 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.
Journal ArticleDOI

Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation

TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.
Journal ArticleDOI

Stability of Protein Pharmaceuticals

TL;DR: Current methodology to stabilize proteins is presented, including additives, excipients, chemical modification, and the use of site-directed mutagenesis to produce a more stable protein species.
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