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Coarse-Grained Model of Entropic Allostery

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Rhoda J. Hawkins, Thomas C. B. McLeish

Biomolecules · Submitted 18 Nov 2003

abstract compiled · 2026-09-23 · no language-model review

The authors' main claim We present a quantitative, coarse-grained model of entropic allostery that suggests design rules for internal cohesive potentials in proteins employing this effect.

how it is stated · hedged possibility 0.95 read the record →

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arXiv IDq-bio/0311023 (version 2)
Pith IDADD26E2V, Pith's permanent record of this paper and its review
CitationRhoda J. Hawkins, Thomas C. B. McLeish. "Coarse-Grained Model of Entropic Allostery." arXiv:q-bio/0311023 (2003). https://pith.science/paper/ADD26E2V
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The paper's own sentences, arranged. Each label is drawn from a closed vocabulary; the number beside it is the probability the classifier gave that label. Numbers in the tables are the authors', checked by code. No sentence in this record was written by a model.

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Compiled by classifier-1.13.0 via TypeSafe API, question bank abstract-p1-20260923, 2026-09-23: 1 request, 4,872 input tokens.

What the abstract itself states, as probabilities: claims first 0.05 · states limitation 0.14 · human participants 0.02 · controlled comparison 0.03 · randomized assignment 0.01 · states quantitative result 0.06 · compares with prior results 0.07 · mentions code or data availability 0.02.

The abstract, sentence by sentence

arXiv listing abstract v2. Results and the main claim are underlined; .

Many signalling functions in molecular biology require proteins bind to substrates such as DNA in response to environmental signals such as the simultaneous binding to a small molecule. Examples are repressor proteins which may transmit information via a conformational change in response to the ligand binding. An alternative entropic mechanism of ``allostery'' suggests that the inducer ligand changes the intramolecular vibrational entropy not just the static structure. We present a quantitative, coarse-grained model of entropic allostery that suggests design rules for internal cohesive potentials in proteins employing this effect. It also addresses the issue of how the signal information to bind or unbind is transmitted through the protein. The model may be applicable to a wide range of repressors and also to signalling in transmembrane proteins.

background contribution method result interpretation main claim

What the classifier reports for each sentence. The number is the probability it gave the label.
#sentencerolethe authors' own workstates the main conclusionstrength
s0 Many signalling functions in molecular biology require proteins bind to substrates such as DNA in response to environmental signals such as the simultaneous binding to a small molecule. background 1.00 0.04 0.02 asserted 0.95
s1 Examples are repressor proteins which may transmit information via a conformational change in response to the ligand binding. background 1.00 0.04 0.02 hedged possibility 0.98
s2 An alternative entropic mechanism of ``allostery'' suggests that the inducer ligand changes the intramolecular vibrational entropy not just the static structure. background 0.99 0.06 0.09 hedged possibility 0.97
s3 We present a quantitative, coarse-grained model of entropic allostery that suggests design rules for internal cohesive potentials in proteins employing this effect. contribution 0.93 0.95 0.62 hedged possibility 0.95
s4 It also addresses the issue of how the signal information to bind or unbind is transmitted through the protein. contribution 0.96 0.80 0.08 asserted 0.89
s5 The model may be applicable to a wide range of repressors and also to signalling in transmembrane proteins. interpretation 0.80 0.30 0.09 hedged possibility 1.00

What kind of paper the classifier reports this is: theoretical result 0.98 · evidence from simulation or computation 0.68.

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  • references and citing sentences
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Every quoted sentence on this record is the authors'. Every label is from Pith's closed vocabulary, with the probability shown beside it. Every number in the measurements table is the authors', checked by code. Record as JSON

The paper
Original abstract

Many signalling functions in molecular biology require proteins bind to substrates such as DNA in response to environmental signals such as the simultaneous binding to a small molecule. Examples are repressor proteins which may transmit information via a conformational change in response to the ligand binding. An alternative entropic mechanism of ``allostery'' suggests that the inducer ligand changes the intramolecular vibrational entropy not just the static structure. We present a quantitative, coarse-grained model of entropic allostery that suggests design rules for internal cohesive potentials in proteins employing this effect. It also addresses the issue of how the signal information to bind or unbind is transmitted through the protein. The model may be applicable to a wide range of repressors and also to signalling in transmembrane proteins.

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