Biomedical subjects

Javaid Shahbaz Khan

Publications and source records attributed to Javaid Shahbaz Khan.

3 recordsLinked to original sources

PubMed2006

Conformational changes of PYP monitored by diffusion coefficient: effect of N-terminal alpha-helices.

Conformational changes in the light illuminated intermediate (pB) of photoactive yellow protein (PYP) were studied from a viewpoint of the diffusion coefficient (D) change of several N-truncated PYPs, which lacked the N-terminal 6, 15, or 23 amino acid residues (T6, T15, and T23, respectively). For intact PYP (i-PYP), D of pB (D(pB)) was approximately 11% lower than that (D(pG)) of the ground state (pG) species. The difference in D (D(pG) - D(pB)) decreased upon cleavage of the N-terminal region in the order of i-PYP>T6>T15>T23. This trend clearly showed that conformational change in the N-terminal group is the main reason for the slower diffusion of pB. This slower diffusion was interpreted in terms of the unfolding of the two alpha-helices in the N-terminal region, increasing the intermolecular interactions due to hydrogen bonding with water molecules. The increase in friction per one residue by the unfolding of the alpha-helix was estimated to be 0.3 x 10(-12) kg/s. The conformational change in the N-terminal group upon photoillumination is discussed.

Bacterial Proteins↗

PubMed2006

Time-resolved thermodynamics: heat capacity change of transient species during photoreaction of PYP.

Heat capacity changes of short-lived transient species in different time ranges were measured for the first time by using the thermal component of the transient grating and transient lens signals at various temperatures. This method was applied to the transient intermediates of Photoactive Yellow Protein (PYP). The temperature dependence of the enthalpy change shows that the heat capacity of the short-lived intermediate pR2 (also called I1 or PYP(L)) species is the same as that of the ground state (pG) species within our experimental accuracy, whereas that of the long-lived intermediate pB (I2 or PYP(M)) is much larger (2.7 +/- 0.4 kJ/mol K) than that of pG. The larger heat capacity is interpreted in terms of the conformational change of the pB species such as melted conformation and/or exposure of the nonpolar residues to the aqueous phase. This technique can be used for photochemical reactions in general to investigate the conformational change and the hydrophobic interaction in a time domain.

Bacterial Proteins↗

PubMed2005

A biosensor in the time domain based on the diffusion coefficient measurement: intermolecular interaction of an intermediate of photoactive yellow protein.

A new type of biosensor is presented for the first time. This method is based on the diffusion measurement in the time domain by the transient grating method. As the first demonstration of this new method, various intermolecular interactions with a reaction intermediate of photoactive yellow protein, such as the protein-protein interaction, protein-DNA interaction, and protein-small molecule binding are detected. The characteristic advantages and limitations are summarized.

Bacterial Proteins↗