Articles written in Journal of Chemical Sciences
Volume 102 Issue 3 June 1990 pp 418-462
Bhaskar G Maiya S M S Chauhan P Bhyrappa V Krishnan P K Bhardwaj Sabyasachi Sarkar Krishna B Pandeya Pavan Mathur Akhil R Chakravarty Birinchi K Das Digambar V Behere Sandeep Modi Samaresh Mitra Sandeep Modi Digambar V Behere Samaresh Mitra Anil Saxena Sandeep Modi Digambar V Behere S Mitra Shyamalava Mazumdar Okhil K Medhi Samaresh Mitra Shyamalava Mazumdar Samaresh Mitra Anup Madan Sandeep Modi Anil Saxena Digamber V Behere S Mitra T Pandiyan M Palaniandavar K L Narayanan H Manohar R Ramaraj C C Thomas S Rajagopal T Rajendra C Srinivasan P Ramamurthy R Roy M C Saha S Panchanan P S Roy C Balagopalakrishna M V Rajasekharan B V Agarwala S Hingorani G A Nagena Gowda Y S Ramaswamy R Halesha N M N Gowda G K N Reddy G C Saxena K L Gupta P Srivastava V D Gupta M Ray R N Mukherjee R N Mohanty K C Dash Ramesh Kapoor S Yadav V Sood P Kapoor B N Anand R Bains Usha K Aggarwal P Garge R Chikate S Padhye J M Savariault P De Loth J P Tuchgues V K Jain M A Vaidya S C Jain S Kalyan Kumar Harkesh B Singh K M Mangaonkar D N Patkar N K Jha Pankaj Sharma S K Date C E Deshpande S D Sathaye S B Deshpande H S Potdar V S Darshane A C Dash R K Nanda N N Das S Gangopadhyay P Banerjee S K Kulshreshtha P S Zacharias N Arulsamy T Ramasami V Subramanian B U Nair M Kanthimathi G Sundararajan V Shivasubramanian R G Bhattacharya S Biswas J Armstrong E M Holt A P Koley
Volume 106 Issue 3 June 1994 pp 763-763
Volume 106 Issue 3 June 1994 pp 766-766
Volume 107 Issue 4 August 1995 pp 497-503
Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region. In metmyoglobin a simple protolytic mechanism associated with alkaline transition involves very small conformational changes.
Volume 107 Issue 4 August 1995 pp 505-518
Detailed pH-dependent steady state and picosecond time-resolved tryptophan fluorescence studies on thiocyanate and azide complexes of horseradish peroxidase have been carried out. The fluorescence decay of the single tryptophan in these species was fitted to a discrete three exponential model. Maximum entropy method analysis also gave three distinct regions of lifetime distributions. The fast subnanosecond lifetime component was found to have > 97% amplitude contribution while other two longer lifetime components have small contributions. Small contributions from the nanosecond lifetime components possibly arise from apoprotein impurity or some small amount of disordered heme conformer of the protein. pH dependence of the fast picosecond lifetime components was found to show a systematic behavior which has been interpreted in the light of obligatory conformation change associated with activation of the enzyme at low pH.
Volume 108 Issue 3 June 1996 pp 313-313 Modern Trends In Inorganic Chemistry
Volume 110 Issue 5 October 1998 pp 479-490 Physical And Theoretical
The unfolding of the membrane protein, cytochrome
Volume 112 Issue 3 June 2000 pp 340-340
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