Residual structure and dynamics in DMSO-d6 denatured dynein light chain protein

Chakraborty, Swagata ; Krishna Mohan, P. M. ; Hosur, Ramakrishna V. (2012) Residual structure and dynamics in DMSO-d6 denatured dynein light chain protein Biochimie, 94 (1). pp. 231-241. ISSN 0300-9084

Full text not available from this repository.

Official URL:

Related URL:


Structural and motional features in the denatured state of a protein dictate the early folding events starting from that state and these features vary depending upon the nature of the denaturant used. Here, we have attempted to decipher the early events in the folding of Dynein Light Chain protein (DLC8), starting from DMSO-d6 denatured state. Multinuclear NMR experiments were used to obtain the full spectral assignment. The HSQC spectrum shows the presence of two sets of peaks for the residues Met 1, Ser 2, Arg 4, Ala 11, Met 17, Thr 26, Lys 44, Tyr 50, Asn 51, Trp 54, His 55, Val 58, Gly 59, Ser 64, Tyr 65, His 68, Phe 86, Lys 87 indicating the presence of slow conformational transition in the heterogeneous ensemble. Analysis of residual structural propensities with secondary 13C chemical shifts, 3J(HN-Hα) coupling constants and 1H-1H NOE revealed the presence of local preferences which encompass both native and non-native like structures. The spectral density calculations, as obtained from measured R1, R2 and 1H-15N steady state NOE values provide insights into the backbone dynamics on the milli to picosecond timescale. The segment Ser 14 - His 55 exhibits slow motions on the milli- to microsecond timescale arising from conformational exchange. The presence of native like structural preference, as well as conformational exchange classifies the above segment as the nucleation site of folding. Based on the observations, we propose here, the probable hierarchy of folding of DLC8 on dilution of denaturant: the two helices are formed first followed by the formation of β2 and β5.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Denatured State; Dynein Light Chain; Dimethyl Sulfoxide; Residual Structure; Conformational Exchange; Folding Initiation Site
ID Code:80113
Deposited On:31 Jan 2012 04:25
Last Modified:31 Jan 2012 04:25

Repository Staff Only: item control page