How ionic strength changes peptide interactions
Understand ionic strength, charge screening and specific-ion effects without treating every salt at the same concentration as chemically equivalent.
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Explore peptide science, analytical testing and the documentation behind research materials.
500 articles to explore
Amphipathic peptides and molecular surfaces
Distinguish mixed polar/non-polar composition from the spatial pattern of an amphipathic peptide, and interpret helical-wheel and hydrophobic-moment diagrams.
Read the article →Why peptide solubility cannot be inferred from length alone
Understand which molecular and environmental features a residue count leaves out, and distinguish a solubility prediction from a result for a specific sample.
Read the article →How metal binding can change peptide structure
Understand how coordination can alter a chain's conformational possibilities, and distinguish metal detection, binding evidence and an observed structural change.
Read the article →Primary, secondary and tertiary structure in short peptides
Separate a peptide's sequence, local backbone arrangement and overall fold, and understand why a short chain need not display every level as a stable structure.
Read the article →Alpha helices in peptide research
Read alpha-helix geometry, residue spacing and structural context without assuming that a helical drawing proves a peptide remains helical in every environment.
Read the article →Beta sheets and peptide assembly
Distinguish beta strands, sheets and larger assemblies, including strand direction, alignment and why a beta-sheet result alone does not identify an amyloid fibril.
Read the article →Beta turns and hairpins
Distinguish a local beta turn from a larger beta hairpin, read residue numbering correctly, and assess what a compact structural motif actually establishes.
Read the article →Intrinsically disordered peptides
Understand conformational ensembles, local preferences and condition-dependent disorder without equating the absence of a single fold with damage or inactivity.
Read the article →Cis-trans isomerisation in peptide backbones
Locate the peptide bond described as cis or trans, distinguish bond conformation from residue chirality, and separate conformer populations from exchange rates.
Read the article →Linear and cyclic peptide topology
Trace peptide connectivity, distinguish head-to-tail cyclisation from side-chain bridges, and avoid confusing a folded loop with a covalently closed ring.
Read the article →Disulfide connectivity and alternative folds
Read cysteine pairing maps, distinguish bond count from connectivity, and understand why equal masses or a shared cysteine framework do not identify one fold.
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