Thermodynamics of Unfolding of β-Trypsin at pH 2.8

Brumano, Maria Helena Nasser; Rogana, E; Swaisgood, Harold E.

doi:10.1006/abbi.2000.1983

Cited by 14 publications

(4 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Stability was assayed in 0.1 M formic acid to keep enzymes inactive(Bittar et al, 2003; Brumano et al, 2000). The fluorescence (excitation at 295 nm/emission at 340 nm) was measured in the range of 4° C to 85° C (at a rate of 4° C/min; sampling interval 0.1° C for most proteins) in a 3 ml quartz cuvette with stirring.…”

Section: Methodsmentioning

confidence: 99%

Protein Sectors: Evolutionary Units of Three-Dimensional Structure

Halabi

Rivoire

Leibler

et al. 2009

Cell

686

1,092

View full text Add to dashboard Cite

Proteins display a hierarchy of structural features at primary, secondary, tertiary, and higher-order levels, an organization that guides our current understanding of their biological properties and evolutionary origins. Here, we reveal a structural organization distinct from this traditional hierarchy by statistical analysis of correlated evolution between amino acids. Applied to the S1A serine proteases, the analysis indicates a decomposition of the protein into three quasi-independent groups of correlated amino acids that we term “protein sectors”. Each sector is physically connected in the tertiary structure, has a distinct functional role, and constitutes an independent mode of sequence divergence in the protein family. Functionally relevant sectors are evident in other protein families as well, suggesting that they may be general features of proteins. We propose that sectors represent a structural organization of proteins that reflects their evolutionary histories.

show abstract

Section: Methodsmentioning

confidence: 99%

Protein Sectors: Evolutionary Units of Three-Dimensional Structure

Halabi

Rivoire

Leibler

et al. 2009

Cell

686

1,092

View full text Add to dashboard Cite

show abstract

“…The pre-exponential factor (A0) of protein inactivation is 9.75×10 38 s -1 and activation energy is 244.05 kJ mol -1 for α-chymotrypsin [19]. For other proteins, the Arrhenius kinetic parameters were derived from literature [35][36][37][38][39][40][41].…”

Section: Protein Inactivation Calculated By Arrhenius Modelmentioning

confidence: 99%

Computational Investigation of Protein Photoinactivation by Molecular Hyperthermia

Kang

Xie

Fall

et al. 2020

Journal of Biomechanical Engineering

View full text Add to dashboard Cite

To precisely control protein activity in a living system is a challenging yet long-pursued objective in biomedical sciences. Recently we have developed a new approach named molecular hyperthermia (MH) to photoinactivate protein activity of interest without genetic modification. MH utilizes nanosecond laser pulse to create nanoscale heating around plasmonic nanoparticles to inactivate adjacent protein in live cells. Here we use a numerical model to study important parameters and conditions for MH to efficiently inactivate proteins in nanoscale. To quantify the protein inactivation process, the impact zone is defined as the range where proteins will be inactivated by nanoparticle localized heating. Factors that reduce the MH impact zone include stretching the laser pulse duration, temperature-dependent thermal conductivity (versus constant properties), and non-spherical nanoparticle geometry. In contrast, the impact zone is insensitive to temperature-dependent material density and specific heat, as well as thermal interface resistance based on reported data. The low thermal conductivity of cytoplasm increases the impact zone. Different proteins with various Arrhenius kinetic parameters have significantly different impact zones. This study provides guidelines to design the protein inactivation process in MH.

show abstract

“…The enthalpy DH for the unfolding is the van't Hoff enthalpy at T m . [49][50][51] The C1 band frequency andintensity, C + 1 0 band intensity, and CRC band frequency and intensity were fitted to the twostate model, and fitting curves are shown in Fig. 3.…”

Section: Two-state Modelmentioning

confidence: 99%