Restriction in the conformational flexibility of apoproteins in the presence of organic cosolvents: a consequence of the formation of "native-like conformation".

Acharya, A S; Iyer, K S; Sahni, G; Khandke, K M; Manjula, B N

Acharya, A S; Iyer, K S; Sahni, G; Khandke, K M; Manjula, B N.

Affiliation

Acharya AS; Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10641.

J Protein Chem ; 11(5): 527-38, 1992 Oct.

Article in En | MEDLINE | ID: mdl-1333215

Subject(s)

Antigens, Bacterial; Apoproteins/chemistry; Bacterial Outer Membrane Proteins; Carrier Proteins; Solvents/pharmacology; 1-Propanol/pharmacology; Bacterial Proteins/chemistry; Cytochrome c Group/chemistry; Cytochromes c; Globins/chemistry; Globins/metabolism; Hydrogen-Ion Concentration; Protein Conformation/drug effects; Protein Structure, Secondary/drug effects; Ribonuclease, Pancreatic/chemistry; Ribonuclease, Pancreatic/metabolism; Serine Endopeptidases/metabolism; Spectrometry, Fluorescence; Temperature; Trypsin/metabolism; Tryptophan/chemistry

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Collection: 01-internacional Database: MEDLINE Main subject: Apoproteins / Solvents / Bacterial Outer Membrane Proteins / Carrier Proteins / Antigens, Bacterial Language: En Journal: J Protein Chem Year: 1992 Document type: Article

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