Light Scattering: a Novel Approach to Analyze Protein 4.1R FERM Domain Interaction with Inside-out-vesicles in Solution

Shiba, Kohei; Nunomura, Wataru; Takakuwa, Yuichi

doi:10.2116/analsci.28.613

Cited by 3 publications

(3 citation statements)

References 18 publications

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“…Because of recent improvements in instrument sensitivity, even proteins that produce weak light scattering intensity can be studied using DLS measurements [13][14]. Furthermore, the polydispersity obtained from DLS measurement is often used as a parameter for predicting protein crystal formation [15][16], indicating that DLS measurements can be adapted to study amyloid fibril formation.…”

Section: Introductionmentioning

confidence: 99%

“…DLS, a technique used to measure protein diffusion due to Brownian motion, was used to evaluate amyloid fibril formation via the change in hydrodynamic diameter that accompanies fibril extension or unfolding in the presence of denaturants such as urea [8][9][10][11][12]. Because of recent improvements in instrument sensitivity, even proteins that produce weak light scattering intensity can be studied using DLS measurements [13][14]. Furthermore, the polydispersity obtained from DLS measurement is often used as a parameter for predicting protein crystal formation [15][16], indicating that DLS measurements can be adapted to study amyloid fibril formation.…”

Section: Introductionmentioning

confidence: 99%

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Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Saiki

Shiba²,

Okumura

2015

FEBS Letters

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a b s t r a c tAmyloid fibrils are fibrous protein assemblies with distinctive cross-b structures. For amyloidosis, there are disease-associated mutations outside of the cross-b structures. Thus, it is necessary to elucidate the role of peripheral sequences outside the cross-b structure. Amyloid fibrils are generally 10 nm in width; however, the amyloid fibrils of truncated barnase M1 peptides missing the Cterminal sequence outside the cross-b structure are 20 nm in width. In this study, we performed comparative analysis of the structural stability of amyloids formed by the respective peptides. We found that the C-terminal amino acids dramatically affect the conformational instability in the presence of a denaturing reagent.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Saiki

Shiba²,

Okumura

2015

FEBS Letters

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“…Recent studies have shown that DLS can be used to evaluate proteins, even those yielding weak light scattering intensities [7,8]. In addition, the polydispersity determined using DLS analysis is often used as a parameter for predicting the formation of protein crystals.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the structural stability of amyloid fibrils by dynamic light scattering

Saiki

Akimoto

2015

J Biorheol

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Amyloid fibrils, formed by protein mis-folding, consist of consecutive hydrogen bonds situated between β-strands. To date, experimental data indicate that amyloid fibrils are structured according to the cross-β structure model, wherein β-strands are oriented perpendicular to the fibril axes. Amyloid fibrils are generally 10 nm in width; however, barnase M1 variants are 20 nm in width. In this study, we performed a comparative analysis of the structural stability of amyloid formation by barnase M1 variants. Based on the results of dynamic light scattering, we propose that the presence or absence of C-terminal amino acids in barnase M1 is dependent on resistance to urea.

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Conserved and unique thermodynamic properties of lactate dehydrogenases in an ectothermic organism, the teleostMicrostomus achne, and an endothermic organism, bovine

et al. 2016

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It is widely believed that enzymatic activities in ectothermic organisms adapt to environmental temperatures. However, to date, no study has thoroughly compared multiple thermodynamic enzymatic characteristics across species living in dramatically different environments. To start to address this gap, we compared the characteristics of lactate dehydrogenase (LDH) purified from the muscles from slime flounder Microstomus achne white muscle and bovine skeletal muscle (bM) and heart. The K and V for pyruvate reduction were about three times higher for M. achne LDH than bM Surprisingly, maximum LDH activity was observed at ∼30 °C and ∼50 °C for M. achne and bovine LDHs, respectively, suggesting that the maximum enzymatic activity of LDH is set at a temperature ∼20 °C higher than environmental or body temperature across species. Although K and V values of these LDHs increased with temperature, the V /K ratio for M. achne LDH and bM was independent. Differential scanning calorimetry and enthalpy change measurements confirmed that M. achne and bovine muscle-specific LDHs shared similar properties. Based on the present findings and previous reports, we hypothesize that the function and thermodynamic properties of muscle LDH are highly conserved between a teleost adapted to cold, M. achne, and bovine.

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Light Scattering: a Novel Approach to Analyze Protein 4.1R FERM Domain Interaction with Inside-out-vesicles in Solution

Cited by 3 publications

References 18 publications

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross‐β region

Evaluation of the structural stability of amyloid fibrils by dynamic light scattering

Conserved and unique thermodynamic properties of lactate dehydrogenases in an ectothermic organism, the teleostMicrostomus achne, and an endothermic organism, bovine

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