De novo design and structural characterization of proteins and metalloproteins
▪ Abstract De novo protein design has recently emerged as an attractive approach for
studying the structure and function of proteins. This approach critically tests our …
studying the structure and function of proteins. This approach critically tests our …
Minimal model systems for β-sheet secondary structure in proteins
SH Gellman - Current Opinion in Chemical Biology, 1998 - Elsevier
Use of model systems to explore the forces that control β sheet formation was stymied for
many years by the perception that small increments of β sheet necessarily aggregate …
many years by the perception that small increments of β sheet necessarily aggregate …
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
AM Fernandez-Escamilla, F Rousseau… - Nature …, 2004 - nature.com
We have developed a statistical mechanics algorithm, TANGO, to predict protein
aggregation. TANGO is based on the physico-chemical principles of β-sheet formation …
aggregation. TANGO is based on the physico-chemical principles of β-sheet formation …
PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues
Background In the past, many methods have been developed for peptide tertiary structure
prediction but they are limited to peptides having natural amino acids. This study describes a …
prediction but they are limited to peptides having natural amino acids. This study describes a …
Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
E Lacroix, AR Viguera, L Serrano - Journal of molecular biology, 1998 - Elsevier
The information about the conformational behavior of monomeric helical peptides in
solution, as well as the α-helix stability in proteins, has been previously utilized to derive a …
solution, as well as the α-helix stability in proteins, has been previously utilized to derive a …
Side-chain effects on peptidyl-prolyl cis/trans isomerisation
U Reimer, G Scherer, M Drewello, S Kruber… - Journal of molecular …, 1998 - Elsevier
Peptidyl-prolyl cis/trans isomerisation has been frequently found as a rate limiting step in the
folding of proteins. In order to determine whether the nature of the amino acid preceding …
folding of proteins. In order to determine whether the nature of the amino acid preceding …
Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
SB Padrick, AD Miranker - Biochemistry, 2002 - ACS Publications
Islet amyloid polypeptide (IAPP) contributes to the pathogenesis of type II diabetes by
depositing as cytotoxic amyloid fibers in the endocrine pancreas. Fiber formation occurs with …
depositing as cytotoxic amyloid fibers in the endocrine pancreas. Fiber formation occurs with …
AHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides
R Kumar, K Chaudhary, M Sharma… - Nucleic acids …, 2015 - academic.oup.com
Abstract AHTPDB (http://crdd. osdd. net/raghava/ahtpdb/) is a manually curated database of
experimentally validated antihypertensive peptides. Information pertaining to peptides with …
experimentally validated antihypertensive peptides. Information pertaining to peptides with …
Design of a 20-amino acid, three-stranded β-sheet protein
T Kortemme, M Ramı́rez-Alvarado, L Serrano - Science, 1998 - science.org
A 20-residue protein (named Betanova) forming a monomeric, three-stranded, antiparallel β
sheet was designed using a structural backbone template and an iterative hierarchical …
sheet was designed using a structural backbone template and an iterative hierarchical …
Structure–function–folding relationship in a WW domain
Protein folding barriers result from a combination of factors including unavoidable energetic
frustration from nonnative interactions, natural variation and selection of the amino acid …
frustration from nonnative interactions, natural variation and selection of the amino acid …