George D. Rose
Department of Biophysics
Johns Hopkins University
Jenkins Hall
3400 N. Charles Street
Baltimore, MD 21218
Phone: (410) 516-7244 Fax: 516-4118
grose @ jhu.edu (delete spaces)
George Rose is a Krieger-Eisenhower Professor of Biophysics and Director of the Institute
for Biophysical Research. His research is focused on protein and
RNA folding, and his research tool is a computer.
The lab's main contributions involve these topics:
- Hierarchic organization of proteins/hierarchic condensation
- the observation that proteins of known structure can be subdivided iteratively into domains and
subdomains prompts the hypothesis that this hierarchic architecture originates in the unfolded state,
where sterically-imposed conformational bias induces chain organization. Under folding conditions,
pre-organized regions of the chain undergo mutually stabilizing self-interactions, leading to incremental
acquistion of structure.
- Hydrogen bonding - the pivotal role of backbone hydrogen bonds
in protein folding.
- Hydrophobic effect and the hydrophobicity profile
- a plot of local hydrophobicty versus residue number, useful in predicting chain turns, antigenic sites,
interior/exterior regions, membrane-spanning helices, etc. from sequence alone.
- The Ω-loop - a class of
non-repetitive secondary structure. Along with α-helices, β-sheet, and tight turns,
Ω-loops account for approximately 95% of all protein structure.
- Helix capping - motifs that provide partners for the
otherwise unsatisfied H-bond donors and acceptors at α-helix terminii, thereby stabilizing the helix.
- Turns in proteins - turns are sites at which a protein changes
its overall chain direction.
- Secondary structure determines tertiary structure - calculations and simulations
showing that knowledge of protein secondary structure (including turns and polyproline II) is sufficient to generate
the three-dimensional structure.
- Unfolded state - a reassessment of the view that the
unfolded state of a polypeptide chain is a statistical coil that visits an
astronomical number of conceivable conformers.
- Conformational entropy - When accessible states are not
equi-probable and their total number is small, entropy can promote organzation,
contrary to the conventional view.
- Physical basis for protein secondary structure - A
physico-chemical theory for protein secondary structure that is not based
on empirical statistics or patterns extracted from a database.
- LINUS - a Monte Carlo program to predict protein structure
from sequence alone.
- Polyproline II - left-handed helix that is a
major component of the unfolded population.
- A conformational map for RNA - a Ramachandran-type map for
RNA.