Structure-function studies of Murraya koenigii trypsin inhibitor revealed a stable core beta sheet structure surrounded by α-helices with a possible role for α-helix in inhibitory function

International Journal of Biological Macromolecules

Volumn 41, Issue 4, 2007, Pages 410-414

  Shee, Chandan ^a   Islam, Asimul ^b   Ahmad, Faizan ^b   Sharma, Ashwani K ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY ROORKEE   (India)

^b JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

Author keywords

Murraya koenigii trypsin inhibitor; Proteolytic stability; Structure function studies

Indexed keywords

PROTEINASE; TRYPSIN INHIBITOR;

ALPHA HELIX; ARTICLE; FLUORESCENCE; MELTING POINT; MURRAYA; PROTEIN DEGRADATION; PROTEIN FUNCTION; STRUCTURE ACTIVITY RELATION; TEMPERATURE SENSITIVITY;

MURRAYA KOENIGII;

EID: 34548244111     PISSN: 01418130     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2007.05.011     Document Type: Article

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