Download Amino acids

Survey
yes no Was this document useful for you?
   Thank you for your participation!

* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project

Document related concepts

Ubiquitin wikipedia , lookup

Protein design wikipedia , lookup

Structural alignment wikipedia , lookup

Bimolecular fluorescence complementation wikipedia , lookup

Protein purification wikipedia , lookup

Homology modeling wikipedia , lookup

Proteomics wikipedia , lookup

Protein moonlighting wikipedia , lookup

Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup

Protein domain wikipedia , lookup

Protein folding wikipedia , lookup

Western blot wikipedia , lookup

Circular dichroism wikipedia , lookup

List of types of proteins wikipedia , lookup

Protein–protein interaction wikipedia , lookup

Protein mass spectrometry wikipedia , lookup

Protein wikipedia , lookup

Intrinsically disordered proteins wikipedia , lookup

Cyclol wikipedia , lookup

Alpha helix wikipedia , lookup

Protein structure prediction wikipedia , lookup

Transcript
Amino acids
by Jana Burianová, Joe Kalivoda
Amino acids classes
Basic classes:
• coded
» essential
» nonessential
• uncoded
• according to their capacity to interact with
water
•
•
•
•
Nonpolar
Polar
Acidic
Basic
Sources of A. A.
• metabolism (most plants,
microbes)
• food (essential A. A.)
Main funtions of A. A.
A. A. are monomers for:
• peptides (2 - 100 units of A. A.)
• oligopeptides (2 – 10 A. A.)
• polypeptides (10 – 100 A. A.)
• proteins (100 & more)
•
•
•
•
structure (simple, composite)
form (fibrilar, globular)
solubility (scleroproteins, albumins, histones, globulins)
function (proteins of basic metabolism, specialized cells)
Structure of:
Peptid
Protein
Polypeptide bond
• peptide bonds are amide linkages between the αcarboxyl group of one AA and the α-amino group of
another AA
Protein structure
• primary (specific amino acid sequence; the order in
which the amino acids are linked together (specified by
genetic information)
• secondary (Consists of several repeating patterns in a
part of polypeptide chain α – helix, b – pleated sheet)
• tertiary (unique three-dimensional conformation that
globular proteins assume as a consequence of the noncovalent interactions between the side chains in their
primary structure)
• quarternary (Many proteins are composed of several
polypeptide chains = subunits)
Origin
•
•
•
•
Biochemistry I doc.RNDr. Ivana Márová, CSc.
Biochemie I doc.RNDr. Ivana Márová, CSc.
Lesson 12 (R/studenti/3. ročník/odborná angličtina)
www.mcdonalds.cz