Hauke Lilie mainly focuses on Biochemistry, Protein folding, Protein structure, Biophysics and Escherichia coli. His study in Biochemistry focuses on Heat shock protein, Chaperone, Binding site, Hsp90 and Mutant. His Protein folding research incorporates themes from Folding, Dimer, Chemical modification, Muramidase and Solubility.
Hauke Lilie has included themes like Native state and Proteolysis in his Protein structure study. As a part of the same scientific study, he usually deals with the Biophysics, concentrating on In vitro and frequently concerns with Protein sequencing and Protein engineering. His work on Inclusion bodies as part of general Escherichia coli study is frequently connected to Molecular physiology, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
The scientist’s investigation covers issues in Biochemistry, Biophysics, Stereochemistry, Protein folding and Protein structure. All of his Biochemistry and Chaperone, Escherichia coli, Enzyme, Recombinant DNA and Isomerase investigations are sub-components of the entire Biochemistry study. As part of the same scientific family, he usually focuses on Biophysics, concentrating on In vitro and intersecting with In vivo and Capsomere.
His research investigates the connection with Stereochemistry and areas like Protease which intersect with concerns in Aryl. His Protein folding research includes elements of Crystallography, Native state, Folding and Solubility. His Protein structure research is multidisciplinary, relying on both Binding domain and Proteolysis.
Hauke Lilie focuses on Biochemistry, Cell biology, RNA, Biophysics and Capsid. His RNA polymerase, Binding domain, Protomer, Transmembrane domain and Enzyme study are his primary interests in Biochemistry. His Biophysics research is multidisciplinary, incorporating perspectives in Protein structure, Membrane, Biomolecule and Single chain.
His Capsid study combines topics from a wide range of disciplines, such as Inclusion bodies, Recombinant DNA, Escherichia coli and In vitro. His work investigates the relationship between Inclusion bodies and topics such as Protein secondary structure that intersect with problems in Viral entry. His research on Fibril often connects related areas such as Protein folding.
Hauke Lilie mostly deals with Biophysics, Cell biology, Biochemistry, Inner mitochondrial membrane and Membrane. His work deals with themes such as Supramolecular chemistry and Lipid bilayer fusion, which intersect with Biophysics. His work on Signal transduction as part of general Cell biology study is frequently linked to Embryonic morphogenesis, therefore connecting diverse disciplines of science.
Hauke Lilie integrates several fields in his works, including Biochemistry and AAA proteins. His Membrane research is multidisciplinary, incorporating elements of Bacterial outer membrane, MICOS complex and Crista. His Fibril research incorporates elements of In vivo and Protein folding.
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In vitro folding of inclusion body proteins.
Rainer Rudolph;Hauke Lilie.
The FASEB Journal (1996)
Advances in refolding of proteins produced in E. coli
Hauke Lilie;Elisabeth Schwarz;Rainer Rudolph.
Current Opinion in Biotechnology (1998)
Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase: IMPLICATIONS FOR HEAT SHOCK IN VIVO
Ursula Jakob;Hauke Lilie;Ines Meyer;Johannes Buchner.
Journal of Biological Chemistry (1995)
Inclusion bodies: formation and utilisation
Beatrix Fahnert;Hauke Lilie;Peter Neubauer.
Advances in Biochemical Engineering / Biotechnology (2004)
Single-particle tracking of murine polyoma virus-like particles on live cells and artificial membranes.
Helge Ewers;Alicia E. Smith;Ivo F. Sbalzarini;Hauke Lilie.
Proceedings of the National Academy of Sciences of the United States of America (2005)
The Dynamics of Hsp25 Quaternary Structure STRUCTURE AND FUNCTION OF DIFFERENT OLIGOMERIC SPECIES
Monika Ehrnsperger;Hauke Lilie;Matthias Gaestel;Johannes Buchner.
Journal of Biological Chemistry (1999)
RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.
Matthias Gautschi;Hauke Lilie;Ursula Funfschilling;Andrej Mun.
Proceedings of the National Academy of Sciences of the United States of America (2001)
Alternatively folded states of an immunoglobulin.
J Buchner;M Renner;H Lilie;H J Hinz.
Biochemistry (1991)
The pro-sequence facilitates folding of human nerve growth factor from Escherichia coli inclusion bodies.
Anke Rattenholl;Hauke Lilie;Adelbert Grossmann;Anne Stern.
FEBS Journal (2001)
L-Arginine increases the solubility of unfolded species of hen egg white lysozyme.
K Ravi Charan Reddy;Hauke Lilie;Rainer Rudolph;Christian Lange.
Protein Science (2005)
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