Spectroscopic studies reveal conformational flexibility of intrinsically unstructured protein HYPK

ISSN Print: 2153-036X
ISSN Online: 2153-0378
www.scirp.net/journal/jbpc
E-mail: [email protected]

Citations

"Spectroscopic studies reveal conformational flexibility of intrinsically unstructured protein HYPK"
written by Swasti Raychaudhuri, Kamalika Roy Choudhury, Shreoshi Palchoudhuri, Shradha Chopra, Nitai P. Bhattacharyya, Debashis Mukhopadhyay,
published by Journal of Biophysical Chemistry, Vol.2 No.4, 2011

has been cited by the following article(s):

[1]	Structural basis of HypK regulating N-terminal acetylation by the NatA complex
	Nature communications, 2017

[2]	Structural basis of HypK regulating N-terminal acetylation by the NatA complex.
	Nature communications, 2017

[3]	Laser induced autofluorescence in the monitoring of β-mercaptoethanol mediated photo induced proton coupled electron transfer in proteins
	Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2015

[4]	Vibrational Study of Tyrosine Molecule
	Advanced Science Letters, 2015

[5]	Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity
	Journal of biosciences, 2014

[6]	Estudio de la proteína MOPC por espectroscopia de fluorescencia
	REDUCA, 2014

[7]	Biochemical and Structural Characterization of RCR3-AVR2: A Model for Protease-inhibitor Interactions at the Plant-pathogen Interface
	2012

[8]	Biochemical and Structural Characterization of RCR3-AVR2: A Model for Protease-Inhibitor Interactions at the Plant-Pathogen Interface.
	NULL 2012

[1]	Structural basis of HypK regulating N-terminal acetylation by the NatA complex Nature Communications, 2017 DOI:10.1038/ncomms15726

[2]	Laser induced autofluorescence in the monitoring of β-mercaptoethanol mediated photo induced proton coupled electron transfer in proteins Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2015 DOI:10.1016/j.saa.2015.04.096

[3]	Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity Journal of Biosciences, 2014 DOI:10.1007/s12038-014-9442-z

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