Steven A Waldauer
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Explore the profile of Steven A Waldauer including associated specialties, affiliations and a list of published articles.
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10
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222
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Recent Articles
1.
Koziol K, Johnson P, Stucki-Buchli B, Waldauer S, Hamm P
Curr Opin Struct Biol
. 2015 Apr;
34:1-6.
PMID: 25900180
2D-IR spectroscopy has matured to a powerful technique to study the structure and dynamics of peptides, but its extension to larger proteins is still in its infancy, the major limitations...
2.
Waldauer S, Stucki-Buchli B, Frey L, Hamm P
J Chem Phys
. 2014 Dec;
141(22):22D514.
PMID: 25494785
By covalently binding a photoswitchable linker across the binding groove of the PDZ2 domain, a small conformational change can be photo-initiated that mimics the allosteric transition of the protein. The...
3.
Buchli B, Waldauer S, Walser R, Donten M, Pfister R, Blochliger N, et al.
Proc Natl Acad Sci U S A
. 2013 Jul;
110(29):11725-30.
PMID: 23818626
By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can...
4.
Bloem E, Koziol K, Waldauer S, Buchli B, Walser R, Samatanga B, et al.
J Phys Chem B
. 2012 Nov;
116(46):13705-12.
PMID: 23116486
We explore the capability of the azidohomoalanine (Aha) as a vibrational label for 2D IR spectroscopy to study the binding of the target peptide to the PDZ2 domain. The Aha...
5.
Voelz V, Jager M, Yao S, Chen Y, Zhu L, Waldauer S, et al.
J Am Chem Soc
. 2012 Jul;
134(30):12565-77.
PMID: 22747188
Protein folding is a fundamental process in biology, key to understanding many human diseases. Experimentally, proteins often appear to fold via simple two- or three-state mechanisms involving mainly native-state interactions,...
6.
Waldauer S, Hassan S, Paoli B, Donaldson P, Pfister R, Hamm P, et al.
J Phys Chem B
. 2012 Jun;
116(30):8961-73.
PMID: 22724381
Amyloid aggregates are highly ordered fibrillar assemblies of polypeptides involved in a number of neurodegenerative diseases. Very little is known on the pathways of self-assembly of peptides into the final...
7.
Waldauer S, Wu L, Yao S, Bakajin O, Lapidus L
J Vis Exp
. 2012 Apr;
(62).
PMID: 22525257
The process by which a protein folds into its native conformation is highly relevant to biology and human health yet still poorly understood. One reason for this is that folding...
8.
Waldauer S, Bakajin O, Lapidus L
Proc Natl Acad Sci U S A
. 2010 Jul;
107(31):13713-7.
PMID: 20643973
A crucial parameter in many theories of protein folding is the rate of diffusion over the energy landscape. Using a microfluidic mixer we have observed the rate of intramolecular diffusion...
9.
DeCamp S, Naganathan A, Waldauer S, Bakajin O, Lapidus L
Biophys J
. 2009 Sep;
97(6):1772-7.
PMID: 19751683
The protein lambda(6-85) has been implicated in barrierless folding by observations of kinetic relaxation after nanosecond T-jump. In this work we observed folding of this protein after dilution of a...
10.
Waldauer S, Bakajin O, Ball T, Chen Y, DeCamp S, Kopka M, et al.
HFSP J
. 2009 May;
2(6):388-95.
PMID: 19436489
By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rapid kinetic experiments, we have found its unfolded state to be more...