Effects of crowders on protein structure

Range Table - link
Organism Various
Reference Shahid S et al., Size-dependent studies of macromolecular crowding on the thermodynamic stability, structure and functional activity of proteins: in vitro and in silico approaches. Biochim Biophys Acta. 2017 Feb1861(2):178-197. doi: 10.1016/j.bbagen.2016.11.014 p.185 table 2PubMed ID27842220
Primary Source See refs beneath table
Comments P.185 left column bottom paragraph: "In this study [investigators] have summarized results showing whether different sizes of crowding agents bring about any conformational changes to the protein (Table 2). The residue-level examination of the conformations of human serum albumin (HSA) and bovine serum albumin (BSA) in the presence of different crowding agents (ficoll 70, dextran 6 and 40, and PEG 8) was also done [primary source 57]. With almost all of the crowders bringing about quenching of the Trp fluorescence resulted in a considerable modulation in local structure as addressed by the Trp residues."
Entered by Uri M
ID 114210