Biophysical Aspects of Protein Folding.
April 2 until April 6 1997 Storlien, Sweden
The 1997 Winterschool in Biophysics was held in
Storlien, Sweden from April 2 until April 6. The theme of this school was Biophysical
Aspects of protein folding. The school was organized as a part of Stockholm Graduate school in
biophysics a joint program between the Karolinska Institute, the Royal Institute of
Technology and Stockholm University.
The school contained lectures from 8 distinguished speakers as well as by the
participating students. Further, most of the students presented posters, the abstracts of
most of the talks as well as posters can be found in this journal. Both theoretical and
experimental aspects of protein folding was tought at the school.
We are grateful for the financial contributions from, the Wenner Gren Foundation,
Pharmacia & UpJohn and from Stockholm Biophysical Graduate School.
More information about the winter school is available
Organiser, Arne Elofsson email@example.com http://www.biokemi.su.se/~arne/
Tel:+46(0)8-161553 Dept of Biochemistry, Stockholm University
Fax:+46(0)8-153679 10691 Stockholm, Sweden
Abstracts of the 1997 Winter
School in Biophysics
prediction results in CASP2
Domingues F., Floeckner H., Jaritz M. and Sippl M.
The folding and binding kinetics of two
homologous proteins:alpha-lactalbumin and lysozyme.
Thermodynamic characterization of the
partially unfolded state of Ca2+-loaded bovine alpha-lactalbumin: evidence that partial
unfolding can precede Ca2+ release.
dynamics of the HIV1 Protease
B. Ullrich , F. Toelgyesi, Z. Szeltner, L. Polgar and J. Fidy
Effects of Strutural Stability on the
Adsorption of Bacteriophage T4 Lysozyme
An Analytical Approach to Protein
Skorobogatiy Maksim, Hong Guo & Martin Zuckermann.
Protein Surfaces and Solvent
Accessibility: Definition and Prediction
Jan Hansen, Ole Lund, Henrik Nielsen, Hans Henrik Stærfeldt,
and Søren Brunak
strength and pH changes the folding pathway of lysozyme
Folding studies on a model b-meander:
the D1 domain of a copper amine oxidase
chains with random and edited sequences
Thermal unfolding of Sso7d from the hyperthermophile Sulfolobus
Threading As a Tool For Ab Initio Prediction Of 3D Folds Of Proteins:
Possibility And Limitations
Dmitry S. Rykunov
ARE PROTEIN FOLDING INTERMEDIATES CAUSED BY TRANSIENT AGGREGATION ?
Maria Silow, Mia Silow and Mikael Oliveberg,
FOLD RECOGNITION USING ProFIT
Jaritz M., Domingues F., Floeckner H. and Sippl M.
EXCIMER AND MONOMER FLUORESCENCE OF PYRENE LABELED HUMAN CARBONIC
ANHYDRASE II Detection of
residual structure during strong denaturing conditions
P. Hammarström., B. Kalman, U. Carlsson, and B.-H Jonsson
Formation of local asymmetric structures in the slow folding reaction
of human carbonic anhydrase II
Architecture of helix bundle membrane proteins: An analysis of
cytochrome c oxidase from bovine mitochondria
Erik Wallin, Gunnar von Heijne & Arne Elofsson
Mechanism of Protein Folding in vivo
Mechanism of Protein Folding in vitro
Intro to Protein Folding.
INSIGHTS INTO THE MOLECULAR MECHANISMS OF PROTEIN FOLDING AND MISFOLDING.
Sheena E. Radford,
1. Random sequences and unique protein structures
2. How can a protein chain find its unique fold?
3. Introduction to protein structure prediction
LOCAL VS NON-LOCAL INTERACTIONS IN PROTEIN FOLDING AND STABILITY. AN
EXPERIMENTALIST POINT OF VIEW
Artefactual intemediates and broad activation barriers in protein folding
membrane proteins G. von Heijne