Amino Acids and Their Properties

These flashcards cover key concepts related to amino acids, their structures, functions, and biochemical significance as discussed in the lecture.

Serine

An amino acid that plays an important role in the catalytic function of many enzymes and is found in high proportions in silk proteins.

D-serine

A neuromodulator produced in neurons from L-serine, co-activating NMDA receptors.

Threonine

An amino acid with two asymmetric carbon atoms, occurring in four stereoisomeric forms, and involved in posttranslational modifications.

Cysteine

An amino acid similar to serine, containing a sulfhydryl group that is nucleophilic and plays a key role in forming disulfide bonds.

Cystine

A molecule formed when two cysteine residues are joined by a disulfide bond, important for protein folding and stability.

Asparagine

A neutral amino acid with an amide side-chain, significant for hydrogen bond interactions and N-linked glycosylation in proteins.

Posttranslational modifications

Chemical changes to amino acids in proteins that occur after translation, affecting protein function and activity.

Disulfide bonds

Covalent bonds formed between cysteine residues that stabilize protein structure, often found in extracellular proteins.

Ellman's Reagent

A chemical used to quantify free thiol groups in a sample, important for studying cysteine in proteins.

O-linked glycosylation

A type of glycosylation where carbohydrates are added to the hydroxyl group of Serine or Threonine residues.