Protein Denaturation and the Properties of Protein Groups

Anson, M. L.

doi:10.1016/s0065-3233(08)60629-4

Cited by 174 publications

(63 citation statements)

References 65 publications

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“…Mostly there is no mention of hydrophobicity at all-as in an otherwise expert review on denaturation by Anson (1945), for example. Likewise a Cold Spring Harbor Symposium on proteins held in 1950, in contrast to the 1938 symposium cited earlier, makes no mention of hydrophobicity, even though there were papers presented which, when viewed retrospectively, were crying out for interpretation in those terms.…”

Section: General Acceptancementioning

confidence: 99%

How protein chemists learned about the hydrophobic factor

1997

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It is generally accepted today that the hydrophobic force is the dominant energetic factor that leads to the folding of polypeptide chains into compact globular entities. This principle was first explicitly introduced to protein chemists in 1938 by Irving Langmuir, past master in the application of hydrophobicity to other problems, and was enthusiastically endorsed by J.D. Bemal. But both proposal and endorsement came in the course of a debate about a quite different structural principle, the so-called "cyclol hypothesis" proposed by D. Wrinch, which soon proved to be theoretically and experimentally unsupportable. Being a more tangible idea, directly expressed in structural terms, the cyclol hypothesis received more attention than the hydrophobic principle and the latter never actually entered the mainstream of protein science until 1959, when it was thrust into the limelight in a lucid review by W. Kauzmann. A theoretical paper by H.S. Frank and M. Evans, not itself related to protein folding, probably played a major role in the acceptance of the hydrophobicity concept by protein chemists because it provided a crude but tangible picture of the origin of hydrophobicity per se in terms of water structure.

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Section: General Acceptancementioning

confidence: 99%

How protein chemists learned about the hydrophobic factor

1997

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“…Keywords: bacteriophage P22; folding intermediates; inclusion body; protein folding; tailspike protein; temperature-sensitive mutations Experimental evidence accumulated over more than 50 years has demonstrated conclusively that protein folding is a spontaneous and reversible process directed by the amino acid sequence of the folding polypeptide (Anson, 1945;Anfinsen, 1973). However, the rules by which the linear polypeptide sequence determines the folding pathway and the final conformation have remained elusive (Jaenicke, 1988; Seckler & Jaenicke, 1992).…”

Section: Introductionmentioning

confidence: 99%

Mechanism of phage P22 tailspike protein folding mutations

Danner

Seckler

1993

Protein Science

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Temperature-sensitive folding (tsfl and global-tsf-suppressor (su) point mutations affect the folding yields of the trimeric, thermostable phage P22 tailspike endorhamnosidase at elevated temperature, both in vivo and in vitro, but they have little effect on function and stability of the native folded protein. To delineate the mechanism by which these mutations modify the partitioning between productive folding and off-pathway aggregation, the kinetics of refolding after dilution from acid-urea solutions and the thermal stability of folding intermediates were analyzed. The study included five tsf mutations of varying severity, the two known su mutations, and four tsf/su double mutants.At low temperature (10 "C), subunit-folding rates, measured as an increase in fluorescence, were similar for wild-type and mutants. At 25 "C, however, tsf mutations reduced the rate of subunit folding. The su mutations increased this rate, when present in the tsf-mutant background, but had no effect in the wild-type background. Conversely, tsf mutations accelerated, and su mutations retarded the irreversible off-pathway reaction, as revealed by temperature down-shifts after varied times during refolding at high temperature (40 "C). The kinetic results are consistent with tsf mutations destabilizing and su mutations stabilizing an essential subunit folding intermediate.In accordance with this interpretation, tsf mutations decreased, and su mutations increased the temperature resistance of folding intermediates, as disclosed by temperature up-shifts during refolding at 25 "C. The stabilizing and destabilizing effects were most pronounced early during refolding. However, they were not limited to subunit-folding intermediates and were also observable during thermal unfolding of the native protein.Keywords: bacteriophage P22; folding intermediates; inclusion body; protein folding; tailspike protein; temperature-sensitive mutations Experimental evidence accumulated over more than 50 years has demonstrated conclusively that protein folding is a spontaneous and reversible process directed by the amino acid sequence of the folding polypeptide (Anson, 1945;Anfinsen, 1973). However, the rules by which the linear polypeptide sequence determines the folding pathway and the final conformation have remained elusive (Jaenicke, 1988; Seckler & Jaenicke, 1992). Threedimensional structure detected in folding intermediates of a number of proteins, by virtue of experimental techniques developed recently, generally appears stabilized by a subset of the interactions present in the native folded protein (Roder et al

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“…This hypothesis is widely used in modeling protein folding and is known as the two-state model. [78][79][80]. The probability to observe the nucleation after t th scan is then equal to the probability that the tip will successfully stretch the protein after t th trials.…”

Section: Time-lapse Experiment: Data Interpretationmentioning

confidence: 99%

Direct Observation of Amyloid Nucleation under Nanomechanical Stretching

et al. 2013

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Self-assembly of amyloid nanofiber is associated with functional and pathological processes such as in neurodegenerative diseases. Despite intensive studies, stochastic nature of the process has made it difficult to elucidate molecular mechanisms for the key amyloid nucleation. Here, we investigated the amyloid nucleation of silk-elastinlike peptide (SELP) using time-lapse lateral force microscopy (LFM). By repeated scanning a single line on a SELP-coated mica surface, we observed sudden stepwise height increases, corresponds to nucleation of an amyloid fiber. The lateral force profiles followed either a worm-like chain model or an exponential function, suggesting that the atomic force microscopy (AFM) tip stretches a single or multiple SELP molecules along the scanning direction, serves as the template for further selfassembly perpendicular to the scan direction. Such mechanically induced nucleation of amyloid fibrils allows positional and directional control of amyloid assembly in vitro, which we demonstrate by generating single nanofibers at predetermined nucleation sites.

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Protein Denaturation and the Properties of Protein Groups

Cited by 174 publications

References 65 publications

How protein chemists learned about the hydrophobic factor

How protein chemists learned about the hydrophobic factor

Mechanism of phage P22 tailspike protein folding mutations

Direct Observation of Amyloid Nucleation under Nanomechanical Stretching

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