Showing results (51-60 of 122) with videos related to
Sort By:
Pageof 13
Analytical Chemistry|April 20, 2010
Production of ribosome-released nascent proteins with optimal physical propertiesDavid R Ziehr, Jamie P Ellis, Peter H Culviner, et al.Biochemistry|April 2, 1998
Unfolding mechanism of rubredoxin from Pyrococcus furiosusS Cavagnero, Z H Zhou, M W Adams, et al.Biochemistry|November 16, 2006
Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domainCarolina A Vega, Neşe Kurt, Zhongjing Chen, et al.Journal of Biomolecular NMR|July 10, 2004
NMR spectroscopic filtration of polypeptides and proteins in complex mixturesSenapathy Rajagopalan, Charles Chow, Vinodhkumar Raghunathan, et al.Biochemistry|August 8, 1995
Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostabilityS Cavagnero, Z H Zhou, M W Adams, et al.The Journal of Physical Chemistry. B|June 12, 2013
Sub-millisecond chain collapse of the Escherichia coli globin ApoHmpHLi Zhu, Neşe Kurt, Jennifer Choi, et al.Lancet (London, England)|July 1, 2016
What is the private sector? Understanding private provision in the health systems of low-income and middle-income countriesMaureen Mackintosh, Amos Channon, Anup Karan, et al.Biochemistry|September 14, 2000
Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residueC Garcia, C Nishimura, S Cavagnero, et al.Biochemistry|November 29, 2001
Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathwayS Cavagnero, C Nishimura, S Schwarzinger, et al.Protein Science : a Publication of the Protein Society|May 3, 2012
Transient interactions of a slow-folding protein with the Hsp70 chaperone machineryAshok Sekhar, Margarita Santiago, Hon Nam Lam, et al.Pageof 13