Using the two iron catalysts, the researchers were able to take four chiral amino acids — proline, leucine, valine and norvaline — and diversify them into 21
different amino acid structures while preserving their handedness.
Not exact matches
There are tons of
different forms, all of which contain a distinct mix of
amino acids arranged in a unique
structure.
When strung together in a sequence,
amino acids create peptides and proteins with
different 3D
structures and, consequently,
different biological functions.
«This allows us to take one
amino acid structure and convert it into many
different structures that represent
different functionalities, which could ultimately lead to
different biological and physical properties of the peptide,» White said.
Despite the enormous variety of peptides and proteins, there are only twenty natural
amino acids, each with a
different structure and chemical properties.
«Two big advantages to the small - molecule catalysts we've developed are that they are very general — they can work on many
different amino acid and peptide
structures — and they are very easy to use.
«When we looked at the
structures, we realized that there were also some basic
amino acids that projected from a
different part of the RNA - binding domains that could be involved in contacting RNA,» Gavis explained.
They are
amino acid chains, made up from 20
different L - alpha -
amino acids, also referred to as residues, that fold into unique three - dimensional protein
structures.
«What's critical with this and what has never been done before is that a single peptide sequence will work against the toxic versions of a number of
different amyloid proteins and peptides, regardless of their
amino acid sequence or the normal 3 - D
structures.»
Like designs made with Silly String spraying out at
different velocities, the folding of an
amino acid chain into a 3D
structure is somewhat speed - dependent, and slower production could cause the protein to take an altered final form.
Based on this crystal
structure, the active site is localized in a binding pocket formed by at least eight
different amino acid residues, including Val32, Lys47, Glu66, Ile69, Leu70, Thr95, Met98, and Asp164 (Fig. 1A).