Biophysics Facility

Circular dichroism is an excellent tool for the determination of secondary structure of proteins by using their property of differential absorption of the two components of circularly polarized light. Besides secondary structure prediction, another popular application of CD is to determine whether mutation(s) affects its conformation or stability. In addition, it can be used to study protein-protein (macromolecules) and protein-ligand (small molecules) interactions.

Fluorescence Spectroscopy is another powerful technique to understand protein conformation at the tertiary structural level. Intrinsic fluorophores such as Trp, Tyr and Phe residues usually provide this information. However, extrinsic fluorophores are also used in some studies where some specific questions are asked. Fluorescence spectroscopy is an excellent tool to study conformational changes, dynamics, protein folding and stability. It also provides crucial information on protein-protein/ligand interaction and enzyme activity. The Biophysics Facility, ACTREC aims to provide the users with well maintained instruments for an array of different experiments enlisted in the table below.

Along with technically sound instrumentation, ACTREC biophysics facility also provides expertise to assist the user in characterizing the desired molecules if required. Depending on individual requirements, either experiments can be performed for the users or help them to operate these instruments independently with minimal supervision. This service is available for students, research scholars and scientists from various academic institutions as well as industries. The costing of the services for data generation and analysis by CD and fluorescence spectroscopy is tabulated below:

Please refer to the files presented in the hyperlinks for CD and Fluorescence Spectrophotometer sample buffer preparation before preparing your samples.
Forms without incorporating the following detailed information will not be accepted-

• Protein/peptide concentration in µM.
• Buffer composition (should include exact composition of the buffer, the pH and the additives).

For an example,
Protein A = 15 µM
Buffer: 20 mM NaH2PO4/Na2HPO4, 100 mM NaCl, pH 7.2

How to submit the samples: Please fill up the relevant forms as per your requirement. For any queries regarding protocol, mode of payment and other specifications, please write to the facility, briefly describing your requirement.

Mode of Payment: Please make payment along with the samples. Payments are to be made only by crossed demand draft (DD). The DD must be drawn in favour of 'The Director, ACTREC' payable at 'Navi Mumbai'.

Kindly note that only on receipt of the payment along with the samples, they will be registered for analysis and taken up for measurement as per the queue of the users of the instrument concerned. As soon as the analysis is over, the spectra along with the receipt / bill will be sent to the users. Separate samples need to be sent for each experiment.

Click here for download Booking Form

Click here for Quotation form

Kakoli Bose, Ph.D.
Principal Investigator, Bose Lab, Associate Editor: Bioscience Reports, Portland Press, UK,
Advanced Centre for Treatment, Research & Education in Cancer (ACTREC)
Tata Memorial Centre
Room No. KS-138
Plot No.1 & 2, Sector 22
Kharghar, Navi Mumbai - 410 210.
HELLO: (022)27405109

Ms. Chanda Baisane, Scientific Assistant “E”, Operator-In-charge Biophysics Facility
Advanced Centre for Treatment, Research & Education in Cancer (ACTREC)
Tata Memorial Centre
Room No. KS-156
Plot No.1 & 2, Sector 22
Kharghar, Navi Mumbai - 410 210.
HELLO: (022)27405031
E-mail: bpf@actrec.gov.in