Exploration of pH-Dependent Behavior of the Anion Receptor Pocket of Subdomain IIA of HSA: Determination of Effective Pocket Charge Using the Debye–Hückel Limiting Law

2013 ◽  
Vol 118 (1) ◽  
pp. 26-36 ◽  
Author(s):  
Priyanka Bolel ◽  
Shubhashis Datta ◽  
Niharendu Mahapatra ◽  
Mintu Halder
Keyword(s):  
Anion Receptor ◽  
Dependent Behavior ◽  
Ph Dependent

scholarly journals pKa Determination of a Histidine Residue in a Short Peptide Using Raman Spectroscopy

Molecules ◽  
2019 ◽  
Vol 24 (3) ◽  
pp. 405 ◽  
Author(s):  
Brett H. Pogostin ◽  
Anders Malmendal ◽  
Casey H. Londergan ◽  
Karin S. Åkerfeldt
Keyword(s):  
Raman Spectroscopy ◽  
Nmr Spectroscopy ◽  
1H Nmr ◽  
1H Nmr Spectroscopy ◽  
Peptide Sequence ◽  
Short Peptide ◽  
Dependent Behavior ◽  
Pka Determination ◽  
Key Functional Groups

Determining the pKa of key functional groups is critical to understanding the pH-dependent behavior of biological proteins and peptide-based biomaterials. Traditionally, 1H NMR spectroscopy has been used to determine the pKa of amino acids; however, for larger molecules and aggregating systems, this method can be practically impossible. Previous studies concluded that the C-D stretches in Raman are a useful alternative for determining the pKa of histidine residues. In this study, we report on the Raman application of the C2-D probe on histidine’s imidazole side chain to determining the pKa of histidine in a short peptide sequence. The pKa of the tripeptide was found via difference Raman spectroscopy to be 6.82, and this value was independently confirmed via 1H NMR spectroscopy on the same peptide. The C2-D probe was also compared to other Raman reporters of the protonation state of histidine and was determined to be more sensitive and reliable than other protonation-dependent signals. The C2-D Raman probe expands the tool box available to chemists interested in directly interrogating the pKa’s of histidine-containing peptide and protein systems.

Dual physically and chemically cross-linked polyelectrolyte nanohydrogels: Compositional and pH-dependent behavior studies

2020 ◽  
Vol 122 ◽  
pp. 109398 ◽  
Author(s):  
Marjan Ashrafizadeh ◽  
Kam Chiu Tam ◽  
Aliyar Javadi ◽  
Mahdi Abdollahi ◽  
Saeid Sadeghnejad ◽  
...  
Keyword(s):  
Dependent Behavior ◽  
Ph Dependent

Dynamic Study of Insole Materials Simulating Real Loads

1994 ◽  
Vol 15 (6) ◽  
pp. 311-323 ◽  
Author(s):  
Ana-Cruz Garcia ◽  
Juan-Vicente Durá ◽  
José Ramiro ◽  
Juan-Victor Hoyos ◽  
Pedro Vera
Keyword(s):  
Dynamic Testing ◽  
Testing Machine ◽  
Biomechanical Analysis ◽  
Careful Selection ◽  
Treatment And Prevention ◽  
Dependent Behavior ◽  
Energy Absorbing ◽  
Selection Of ◽  
Shoe Inserts

A new methodology of biomechanical analysis of materials for shoe inserts is presented. This methodology is based on the determination of the loads applied to the materials in real situations and its simulation by means of a dynamic testing machine. Both the rigidity and the energy-absorbing characteristics of the materials are investigated as a function of frequency. This methodology is applied to the study of several commercially available viscoelastic materials intended for shoe inserts in the treatment and prevention of degenerative joint diseases. The influence of thickness is investigated as well as the frequency-dependent behavior of the materials studied. Significant differences between materials and different behavior as a function of thickness and frequency were found. Poron materials were found to have the lowest rigidity, good for adequate pressure distribution, while Noene showed the highest energy absorption. A careful selection of the thickness of Sorbothane was found to be necessary for avoiding flattening of the material.

pH-Dependent Behavior of Surface-immobilized Artificial Leucine Zipper Proteins

Langmuir ◽  
2004 ◽  
Vol 20 (18) ◽  
pp. 7747-7752 ◽  
Author(s):  
Molly M. Stevens ◽  
Stephanie Allen ◽  
Jill K. Sakata ◽  
Martyn C. Davies ◽  
Clive J. Roberts ◽  
...  
Keyword(s):  
Leucine Zipper ◽  
Dependent Behavior ◽  
Ph Dependent
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