• Case, David (PI)
  • Hogle, James (PI)
  • Singh, U. (PI)
  • Wilson, Ian (PI)
  • Stout, C. David (PI)
  • Skolnick, Jeffrey (PI)
  • Wright, Peter (PI)
  • Olson, Arthur (PI)

Project Details


This Program Project brings together a group of investigators
which comprises a broad range of experimental and computational
techniques in three-dimensional structure analysis for a concerted
study of the fundamental aspects of protein folding and assembly.
The Program will capitalize on the availability of a core facility
of state-of-the-art computational, computer graphic, x-ray
diffraction and NMR spectroscopy equipment. The research will
approach the question of ordering of protein structure using both
experimental and computational techniques applied to systems
that range from peptide fragments to intact viruses. The
Program represents a new and very significant undertaking within
the department that will utilize the complementary strengths of
the large group of principal investigators and co-investigators to
approach one of the most fundamental problems in molecular
biology. In Project 1, Dr. Case will use molecular dynamics
simulations to study hydrogen bonding in the formation of
characteristic secondary structures in peptide fragments. In
parallel, Dr. Wright's group in Project VI, will explore by NMR
methods the mechanism and dynamics of protein folding and
assembly at the level of peptide fragments. They will study the
influence of amino acid sequence on the stability of secondary
structure of peptides and investigate their folding and
stabilization through interactions at the surface of a folded
carrier protein. At the next level of association, Dr. Stout and
co-investigators in Project IV will examine possible pathways
between two observed tertiary folds seen for a domain of
metallothionein using high pressure crystallography as well as
distance geometry and molecular mechanics. In Project V.
Dr. Wilson will use x-ray crystallography coupled with
immunologic data to understand the nature of protein peptide and
protein-protein association required for recognition and stable
complex formation. By studying a series of antibody complexes a
detailed understanding of epitope organization and recognition
will be gained. In Project II, Dr. Hogle will use a combination of
biological characterization crystallographic studies and molecular
modeling to understand the structural basis for temperature
sensitivity and its dependance on sequence and structure in the
poliovirus. Dr. Olson in Project III will characterize a broad range
of assembled interfaces including those in viruses and antibodies
using computer graphics modeling coupled with calculations of
shape, electrostatic energy, hydrophobicity, and solvent
contributions. By focusing on overlapping system, techniques, and
questions, this Program Project will foster significant
collaborative interactions which will enhance the value of each
individual project.
Effective start/end date7/1/876/30/98


  • National Institutes of Health
  • National Institutes of Health
  • National Institutes of Health
  • National Institutes of Health


  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Explore the research topics touched on by this project. These labels are generated based on the underlying awards/grants. Together they form a unique fingerprint.