Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Nagaraju Chada"'
Autor:
Raghavendar Reddy Sanganna Gari, Gavin M. King, Nagaraju Chada, Krishna P. Sigdel, Brendan P. Marsh
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
Scientific Reports
Scientific Reports
Imaging by atomic force microscopy (AFM) offers high-resolution descriptions of many biological systems; however, regardless of resolution, conclusions drawn from AFM images are only as robust as the analysis leading to those conclusions. Vital to th
Autor:
Linda L. Randall, Raghavendar Reddy Sanganna Gari, Nagaraju Chada, Chunfeng Mao, Brendan P. Marsh, Kanokporn Chattrakun, Gavin M. King
Publikováno v:
Science Advances. 5
Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of active translocases underlie general secretory system function, yet directly visualizing dynamics has been challenging. We imaged ac
Autor:
Raghavendar Reddy, Sanganna Gari, Kanokporn, Chattrakun, Brendan P, Marsh, Chunfeng, Mao, Nagaraju, Chada, Linda L, Randall, Gavin M, King
Publikováno v:
Science Advances
We reveal the dynamic topography of active translocases as a function of precursor, nucleotide, and stage of translocation.
Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of act
Escherichia coli exports proteins via a translocase comprising SecA and the translocon, SecYEG. Structural changes of act
Autor:
Raghavendar Reddy Sanganna Gari, Nagaraju Chada, Linda L. Randall, Gavin M. King, Krishna P. Sigdel, Tina R. Matin
Publikováno v:
Scientific Reports
Though ubiquitous in optical microscopy, glass has long been overlooked as a specimen supporting surface for high resolution atomic force microscopy (AFM) investigations due to its roughness. Using bacteriorhodopsin from Halobacterium salinarum and t
Autor:
Gavin M. King, Linda L. Randall, Krishna P. Sigdel, Tina R. Matin, Chunfeng Mao, Raghavendar Reddy Sanganna Gari, Nagaraju Chada
Publikováno v:
Biophysical Journal. 106:458a
Since its invention in the mid-1980s, the atomic force microscope (AFM) has become an invaluable complementary tool for studying membrane proteins in near-native environments. Historically, mica is the most common substrate utilized for biological AF