I. Roterman

Publications149
h-index24
Citations1,757
Highly Influential Citations21
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Early-Stage Folding in Proteins (In Silico) Sequence-to-Structure Relation
A sequence-to-structure library has been created based on the complete PDB database. The tetrapeptide was selected as a unit representing a well-defined structural motif. Seven structural forms were… Expand
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Self‐assembly of Congo Red—A theoretical and experimental approach to identify its supramolecular organization in water and salt solutions
The supramolecular organization of Congo Red molecules was studied to approach an understanding of the unusual complexation characteristics associated with the liquid crystalline nature of this dye.… Expand
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The structure and protein binding of amyloid-specific dye reagents.
The self-assembling tendency and protein complexation capability of dyes related to Congo red and also some dyes of different structure were compared to explain the mechanism of Congo red binding and… Expand
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Albumin binds self-assembling dyes as specific polymolecular ligands.
Self-assembling dyes with a structure related to Congo red (e.g. Evans blue) form polymolecular complexes with albumin. The dyes, which are lacking a self-assembling property (Trypan blue, ANS) bind… Expand
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Antifreeze proteins
The antifreeze protein (AFP) activity is explained using two models. The first model is using ice binding and the second is using antiice structuralization of water molecules. The description of AFP… Expand
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A comparison of the CHARMM, AMBER and ECEPP potentials for peptides. II. Phi-psi maps for N-acetyl alanine N'-methyl amide: comparisons, contrasts and simple experimental tests.
phi-psi maps of N-acetyl alanine N'-methyl amide have been computed using the CHARMM potential, the all-atom AMBER potential, and the ECEPP/2 potential, before and after adiabatic relaxation. Maps… Expand
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A comparison of the CHARMM, AMBER and ECEPP potentials for peptides. I. Conformational predictions for the tandemly repeated peptide (Asn-Ala-Asn-Pro)9.
A search for low-energy helical and near-helical conformations of the tandemly repeated peptide (Asn-Ala-Asn-Pro)9 was undertaken by minimization of the CHARMM potential energy function from eight… Expand
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Why Congo red binding is specific for amyloid proteins - model studies and a computer analysis approach.
BACKGROUND The complexing of Congo red in two different ligand forms - unimolecular and supramolecular (seven molecules in a micelle) - with eight deca-peptides organized in a b-sheet was tested by… Expand
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Congo red-stabilized intermediates in the lambda light chain transition from native to molten state.
Disruption of tertiary interaction makes a protein accessible to penetration by different small molecular compounds. Their interaction may stabilize the altered protein conformation. Congo red is… Expand
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The geometrical analysis of peptide backbone structure and its local deformations.
A proposal to use a unified description of protein structures is presented, assuming that all peptide chain conformations (including beta-structure) may be considered as helix-derived. In this… Expand
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