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Origins of globular structure in proteins
Author(s) -
Tolstoguzov Vladimir
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00040-x
Subject(s) - globular protein , folding (dsp implementation) , chemistry , protein folding , molecule , polymer , solubility , globular cluster , solvent , crystallography , biophysics , biochemistry , organic chemistry , biology , physics , electrical engineering , quantum mechanics , galaxy , engineering
Thermodynamic incompatibility of polymers in a common solvent is possibly a driving force for formation and evolution of globular protein structures. Folding of polypeptide chains leads to a decrease in both excluded volume of molecules and chemical differences between surfaces of globular molecules with chemical information hidden in the hydrophobic interior. Folding of polypeptide chains results in ‘molecular or thermodynamic mimicry' of globular proteins and in at least more than 10‐fold higher phase separation threshold values of mixed protein solutions compared to those of classical polymers. Unusually high co‐solubility might be necessary for efficient biological functioning of proteins, e.g. enzymes, enzyme inhibitors, etc.