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The molten globular intermediate form in the folding pathway of human carbonic anhydrase B
Author(s) -
Jagannadham M.V.,
Balasubramanian D.
Publication year - 1985
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 - 10.1016/0014-5793(85)80396-3
Subject(s) - guanidinium chloride , molten globule , globular protein , carbonic anhydrase , chemistry , folding (dsp implementation) , enzyme , carbonic anhydrase ii , globular cluster , protein folding , native state , crystallography , chloride , stereochemistry , biochemistry , organic chemistry , physics , quantum mechanics , galaxy , electrical engineering , engineering
The acid‐induced and guanidinium chloride‐induced conformational transitions in human carbonic anhydrase B have been. analyzed. A structural form was detected at pH 3, which has a higher secondary structural order than the native enzyme but little tertiary structure. The enzyme dissolved in an intermediate concentration of the denaturant guanidinium chloride (1 M at pH 7.5) also adopts a similar conformational state. This form, denoted as the intermediate form I, possesses most of the characteristics defined for the molten globular state of globular proteins and might serve as the embryonic structural intermediate during the self‐organization of the protein into its functional native form.