Jennifer Neumann - Academia.edu (original) (raw)
Papers by Jennifer Neumann
BIOspektrum, 2012
Membrane proteins have complex structures containing multiple structural elements. Using the aqua... more Membrane proteins have complex structures containing multiple structural elements. Using the aquaglyceroporin GlpF of the bacterium Escherichia coli as an example, we highlight individual steps and intermediates in the assembly pathway of a complex membrane protein. Folding of GlpF involves specific transmembrane helix-helix interactions, folding of individual domains and formation of re-entry loops, as well as assembly of a GlpF tetramer, the physiological and functional protein state.
Nucleic acids research, 2014
In the resurging field of RNA modifications, quantification is a bottleneck blocking many excitin... more In the resurging field of RNA modifications, quantification is a bottleneck blocking many exciting avenues. With currently over 150 known nucleoside alterations, detection and quantification methods must encompass multiple modifications for a comprehensive profile. LC-MS/MS approaches offer a perspective for comprehensive parallel quantification of all the various modifications found in total RNA of a given organism. By feeding (13)C-glucose as sole carbon source, we have generated a stable isotope-labeled internal standard (SIL-IS) for bacterial RNA, which facilitates relative comparison of all modifications. While conventional SIL-IS approaches require the chemical synthesis of single modifications in weighable quantities, this SIL-IS consists of a nucleoside mixture covering all detectable RNA modifications of Escherichia coli, yet in small and initially unknown quantities. For absolute in addition to relative quantification, those quantities were determined by a combination of e...
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2015
Aquaporins are highly selective polytopic transmembrane channel proteins that facilitate the perm... more Aquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure can be reached by following different folding pathways. Based on the available data, we suggest a complex folding pathway for aquaporins, starting from the insertion of individual helices up to the formation of the tetrameric aquaporin structure. The consequences of some known mutations in human aquaporin-encoding genes, which most likely affect the folding and stability of human aquaporins, are discussed.
Chemical Communications, 2014
BIOspektrum, 2012
Membrane proteins have complex structures containing multiple structural elements. Using the aqua... more Membrane proteins have complex structures containing multiple structural elements. Using the aquaglyceroporin GlpF of the bacterium Escherichia coli as an example, we highlight individual steps and intermediates in the assembly pathway of a complex membrane protein. Folding of GlpF involves specific transmembrane helix-helix interactions, folding of individual domains and formation of re-entry loops, as well as assembly of a GlpF tetramer, the physiological and functional protein state.
Nucleic acids research, 2014
In the resurging field of RNA modifications, quantification is a bottleneck blocking many excitin... more In the resurging field of RNA modifications, quantification is a bottleneck blocking many exciting avenues. With currently over 150 known nucleoside alterations, detection and quantification methods must encompass multiple modifications for a comprehensive profile. LC-MS/MS approaches offer a perspective for comprehensive parallel quantification of all the various modifications found in total RNA of a given organism. By feeding (13)C-glucose as sole carbon source, we have generated a stable isotope-labeled internal standard (SIL-IS) for bacterial RNA, which facilitates relative comparison of all modifications. While conventional SIL-IS approaches require the chemical synthesis of single modifications in weighable quantities, this SIL-IS consists of a nucleoside mixture covering all detectable RNA modifications of Escherichia coli, yet in small and initially unknown quantities. For absolute in addition to relative quantification, those quantities were determined by a combination of e...
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2015
Aquaporins are highly selective polytopic transmembrane channel proteins that facilitate the perm... more Aquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure can be reached by following different folding pathways. Based on the available data, we suggest a complex folding pathway for aquaporins, starting from the insertion of individual helices up to the formation of the tetrameric aquaporin structure. The consequences of some known mutations in human aquaporin-encoding genes, which most likely affect the folding and stability of human aquaporins, are discussed.
Chemical Communications, 2014