Paul S. Cremer (born 1967) is an American chemist in physical and analytical chemistry at biological interfaces.
Education and academic career
Cremer graduated from
University of Wisconsin-Madison
A university () is an institution of higher (or tertiary) education and research which awards academic degrees in several academic disciplines. ''University'' is derived from the Latin phrase ''universitas magistrorum et scholarium'', which ...
with a BA in 1990, completed his PhD at
University of California, Berkeley
The University of California, Berkeley (UC Berkeley, Berkeley, Cal, or California) is a public land-grant research university in Berkeley, California. Established in 1868 as the University of California, it is the state's first land-grant u ...
in 1996, and completed postdoctoral work at
Stanford University (1996-1998).
Cremer joined the faculty in the chemistry department, Texas A&M University in 1998.
He is known for his work in
Hofmeister series
The Hofmeister series or lyotropic series is a classification of ions in order of their lyotrophic properties, which is the ability to salt out or salt in proteins. The effects of these changes were first worked out by Franz Hofmeister, who stud ...
and supported
lipid bilayers
The lipid bilayer (or phospholipid bilayer) is a thin polar membrane made of two layers of lipid molecules. These membranes are flat sheets that form a continuous barrier around all cells. The cell membranes of almost all organisms and many viru ...
.
Google Scholar Profile
/ref> He is also interested in nanofabrication, sum-frequency generation
Sum-frequency generation (SFG) is a second order nonlinear optical process based on the annihilation of two input photons at angular frequencies \omega_1 and \omega_2 while, simultaneously, one photon at frequency \omega_3 is generated. As with a ...
and biosensing.
Cremer joined the faculty in the chemistry department, Penn State University, in 2013. He continues his research in the lipid bilayer and protein folding
Protein folding is the physical process by which a protein chain is translated to its native three-dimensional structure, typically a "folded" conformation by which the protein becomes biologically functional. Via an expeditious and reprodu ...
.
References
External links
Cremer lab website
Google Scholar Profile
{{DEFAULTSORT:Cremer, Paul
American chemists
Analytical chemistry
University of Wisconsin–Madison alumni
Living people
University of California, Berkeley alumni
Stanford University alumni
Pennsylvania State University faculty
1967 births