De novo design and structural characterization of proteins and metalloproteins

WF DeGrado, CM Summa, V Pavone… - Annual review of …, 1999 - annualreviews.org
▪ 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 …

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 …

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 …

PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues

S Singh, H Singh, A Tuknait, K Chaudhary, B Singh… - Biology direct, 2015 - Springer
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 …

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 …

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 …

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 …

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 …

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 …

Structure–function–folding relationship in a WW domain

M Jäger, Y Zhang, J Bieschke… - Proceedings of the …, 2006 - National Acad Sciences
Protein folding barriers result from a combination of factors including unavoidable energetic
frustration from nonnative interactions, natural variation and selection of the amino acid …