Study of chemically unfolded β-casein by means of small-angle neutron scattering

Aschi, Adel; Gharbi, A.; Daoud, M.; Douillard, Roger; Calmettes, P.

doi:10.1016/j.physb.2006.04.010

Cited by 5 publications

(4 citation statements)

References 31 publications

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“…The influence of the secondary structure on thermal and chemical denatured states has been investigated for different proteins in aqueous solutions: phosphoglycerate kinase (PGK), β-casein, neocarzinostatine (NCS), bovine pancreatic trypsin inhibitor (BPTI), apo-calmodulin, and β-lactoglobulin (βLG) . Recently, the heat-denatured states of apo-calmodulin that is a small, mainly α, soluble protein have been studied.…”

Section: Pressure and Temperature Unfolding Of Proteinsmentioning

confidence: 99%

Water Determines the Structure and Dynamics of Proteins

et al. 2016

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Water is an essential participant in the stability, structure, dynamics, and function of proteins and other biomolecules. Thermodynamically, changes in the aqueous environment affect the stability of biomolecules. Structurally, water participates chemically in the catalytic function of proteins and nucleic acids and physically in the collapse of the protein chain during folding through hydrophobic collapse and mediates binding through the hydrogen bond in complex formation. Water is a partner that slaves the dynamics of proteins, and water interaction with proteins affect their dynamics. Here we provide a review of the experimental and computational advances over the past decade in understanding the role of water in the dynamics, structure, and function of proteins. We focus on the combination of X-ray and neutron crystallography, NMR, terahertz spectroscopy, mass spectroscopy, thermodynamics, and computer simulations to reveal how water assist proteins in their function. The recent advances in computer simulations and the enhanced sensitivity of experimental tools promise major advances in the understanding of protein dynamics, and water surely will be a protagonist.

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Section: Pressure and Temperature Unfolding Of Proteinsmentioning

confidence: 99%

Water Determines the Structure and Dynamics of Proteins

et al. 2016

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“…B ðUÞ 22 has been measured in some instances, but it necessarily must be done under non-native favoring conditions that do not promote aggregation. 119,120 That is, when attempting to predict non-native aggregation, one is interested in B (1), (3), and (4) from the list of colloidal interactions at the beginning of this section. Contributions from (2) are neglected by approximating that they are compensated by solvent-protein van der Waals attractions or are weak compared to hydrophobic interactions.…”

Section: Approaches To Predict Aggregaton Rates and Shelf Life Conformentioning

confidence: 99%

Principles, approaches, and challenges for predicting protein aggregation rates and shelf life

Weiss

Young

Roberts

2009

Journal of Pharmaceutical Sciences

276

289

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“…Schizophylan in 0.01 M NaOH ( L p = 200 nm) [63], DNA in 0.2 M NaCl ( L p = 50 nm) [64], poly(n‐hexyl isocyanate) in hexane ( L p = 42 nm) [65], and nitrocellulose in acetone ( L p = 17 nm) [65], but greater than those for any other semiflexible polymers, e.g. poly(tert‐butyl crotonate) in n‐Butyl chloride ( L p = 5.5 nm) [66], poly(l‐phenyl‐l‐propyne) in cyclohexane ( L p = 3.8 nm) [67] and β‐casein in 4 M guanidine hydrochloride ( L p = 3.1 nm) [68]. This difference may be due to the Flory‐Fox factor, ϕ (ϕ < theoretical value 2.86 × 1023 mol −1 ).…”

Section: Resultsmentioning

confidence: 99%

Study of solution properties of poly(deamino‐tyr‐tyr carbonate hexyl ester) by light scattering and viscometry in dilute and semidilute regime

Aschi

Trabelsi

Gharbi

2010

Polymer Engineering & Sci

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The structure and properties of poly(deamino‐tyr‐tyr carbonate hexyl ester), in dilute and semidilute solutions, were studied using static, dynamic light scattering, and viscometry. The overlap concentration, c* is determined by viscosity. The angular dependence of Zimm plots shows no downturn at low angles. In addition, bimodal distribution curves were computed from the quasielastic measurements. The radius of gyration and the second virial coefficient A2 are found to be respectively 45.8 nm and 9.4 mol cm3 g−2. The correlation and persistence lengths are discussed. The poly (deamino‐tyr‐tyr carbonate hexyl ester) or poly(DTH‐carbonate) chain in THF, at T = 20°C, behaves as a wormlike chain with persistence length. The persistence length obtained using light scattering is compared with that obtained using viscosity with good agreement. These values obtained from these measurements reflect a high degree of local chain persistence. The reduced viscosity in dilute regime provides a value of apparent viscosity hydrodynamic radius three times lower than obtained by static light scattering. POLYM. ENG. SCI., 50:1605–1612, 2010. © 2010 Society of Plastics Engineers

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Study of chemically unfolded β-casein by means of small-angle neutron scattering

Cited by 5 publications

References 31 publications

Water Determines the Structure and Dynamics of Proteins

Water Determines the Structure and Dynamics of Proteins

Principles, approaches, and challenges for predicting protein aggregation rates and shelf life

Study of solution properties of poly(deamino‐tyr‐tyr carbonate hexyl ester) by light scattering and viscometry in dilute and semidilute regime

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