Size-dependent studies of macromolecular crowding on the thermodynamic stability, structure and functional activity of proteins: in vitro and in silico approaches

• Published in: Biochimica et biophysica acta. General subjects Vol. 1861; no. 2; pp. 178 - 197
• Main Authors: Shahid, Sumra, Hassan, Md. Imtaiyaz, Islam, Asimul, Ahmad, Faizan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2017
• Subjects: Animals; Computer Simulation; Crowder size; Excluded volume effect; Functional activity; Humans; in vitro studies; M D simulation; Macromolecular crowding; Macromolecular Substances - chemistry; Protein Conformation; Protein Folding; proteins; Proteins - chemistry; solvents; Structure-Activity Relationship; Thermodynamic stability; Thermodynamics; Km; Functional activity; ANS; HRP; mi-CK; CRABP I; M D simulation; GdmCl; MDH; BSA; LDH; Trp; PDI; bOBP; SPT; HSA; Tm; FRET; Macromolecular crowding; AMPPNP; GN; Thermodynamic stability; Crowder size; GAPD; ΔΔGND; r; PEG; FKBP; ΔHm; Excluded volume effect; kcat; Kd

The environment inside cells in which proteins fold and function are quite different from that of the dilute buffer solutions often used during in vitro experiments. The presence of large amounts of macromolecules of varying shapes, sizes and compositions makes the intracellular milieu extremely cro...