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Cited by 481

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Neutral Salts: The Generality of Their Effects on the Stability of Macromolecular Conformations

von Hippel, Peter H., Wong, Kwok-Ying·1964·Science

Abstract

The effects of various neutral salts on the temperature of the thermally-induced denaturation of the globular protein ribonuclease are described and compared with the effects of these salts on helix-coil transition temperatures in other macromolecules. These agents affect the stability of the native form of macromolecules as diverse as ribonuclease, collagen, DNA, and myosin in very similar ways; salts such as KSCN and CaCl 2 serve as very potent general structural destabilizers or denaturants, while salts such as (NH 4 ) 2 SO 4 and K 2 HPO 4 strongly stabilize the native conformation. The effectiveness of the neutral salts as ribonuclease destabilizers is compared with that of urea and the guanidinium salts.

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Crossref · 10.1126/science.145.3632.577

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Metadata

Authors
von Hippel, P. H., & Wong, K.-Y.
Venue
Science
Published
1964-08-07
Volume
145
Issue
3632
Pages
577-580
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1993588189
Cited by
481
References
7
FWCI
11.75
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Neutral Salts: The Generality of Their Effects on the Stability of Macromolecular Conformations. https://app.cochat.ai/papers/10.1126/science.145.3632.577
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von Hippel, P. H., & Wong, K.-Y. (1964). Neutral Salts: The Generality of Their Effects on the Stability of Macromolecular Conformations. Science. https://doi.org/10.1126/science.145.3632.577

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.