Protein structure and dynamics at high pressure

Heat Shock Protein-Mediated Resistance to High Hydrostatic Pressure in Escherichia coli

“…At a more fundamental level, several studies have provided information on specific cellular targets of HHP in an attempt to identify the ultimate cause(s) of cellular inactivation. Many in vitro studies with purified proteins and with membrane vesicles have indicated that HHP can cause protein denaturation and affect membrane fluidity, effects which were predicted from thermodynamic principles (3,18). Most in vivo observations on living cells exposed to HHP can be linked to these two effects: inhibition of key enzymes (43,49); and inactivation of cellular structures and processes, including transcription (9), ribosomes (39), microtubules (33) and membrane proteins (46), and structural and functional disruption of the cell membrane (11,42).…”

Solvent effects on the molecular structures of crude gliadins as revealed by density and ultrasound velocity measurements

“…According to the definition of compressibility, the compressibility coefficient, β, which is used more widely, can be defined as the pressure dependence of the relative volume (Gavish et al, 1983;Bloor et al, 1983;Cooper, 1984;Heremans and Smeller, 1998;Blandamer et al, 2001;Taulier et al, 2005):…”

“…For aqueous solutions the difference between β S and β T is small so that it does not exceed a few percent because of the large value of C p and the small value of thermal expansibility coefficient for water (Millero et al, 1976;Hoiland, 1980;Gekko and Hasegawa, 1986;Gekko and Hasegawa, 1989;Sarvazyan, 1991;Tikhonov et al, 1995;Povey, 1997;Heremans and Smeller, 1998;Taulier and Chalikian, 2002).…”

“…Thus, from equation 7, the value of β S is obtained as (Gekko and Noguchi, 1974;Gekko and Noguchi, 1979;Sarvazyan et al, 1979;Chavez et al, 1985;Gekko and Hasegawa, 1986;Sarvazyan, 1991;Chalikian et al, 1992;Kharakoz and Sarvazyan, 1993;Chalikian et al, 1994a;McClements, 1995;Tikhonov et al, 1995;Paci and Marchi, 1996;Hianik et al, 1997;Pinfield and Povey, 1997;Povey, 1997;Heremans and Smeller, 1998;Povey, 1998;Burakowski and Gliński, 2007;Raman et al, 2007).…”

“…calculated the unit compressibility contributions of charged, cha γ , polar, pol γ , and non-polar, non γ , protein surface area from 18 °C to 55 °C in aqueous solutions. The negative values of unit compressibility contributions shown in Table 2.1 indicate that the interaction between the solvent (23) molecules and proteins contributes negatively to the protein compressibility properties (Gekko and Noguchi, 1979;Gekko and Hasegawa, 1986;Gekko and Hasegawa, 1989;Gekko and Yamagami, 1991;Kharakoz, 1991;Kharakoz and Sarvazyan, 1993;Paci and Marchi, 1996;Kharakoz, 1997;Heremans and Smeller, 1998;Gekko, 2002;Taulier and Chalikian, 2002;Valdez et al, 2001;Chalikian, 2003;Gekko et al, 2003;Marchi, 2003;Gekko et al, 2004;Bano and Marek, 2006;Dadarlat and Post, 2006;Mori et al, 2006). pol γ -66 ± 3 -62 ± 3 -60 ± 3 -58 ± 3 -57 ± 3 non γ -13 ± 2 -9 ± 2 -6 ± 2 -5 ± 2 -4 ± 2 compared the unit compressibility contribution of charged, cha γ , polar, pol γ , and non-polar, non γ , protein surfaces with those on low-molecular-mass compounds to illustrate the hydration properties of proteins.…”