BIO 320 Lecture Notes - Lecture 3: Glycosylation, Methylation, Atp Hydrolysis
Document Summary
The folding of a protein is controlled by its amino acid sequence, involving mostly the 4 types of noncovalent interactions between (backbone and r groups of pairs of) amino acids. Thermal energy within a cell is critical for proper folding of proteins. Proteins fold into a conformation of lowest energy. Secondary structures, involving relatively short range interactions. Nascent proteins fold (often quickly) into an initial structure (molten globule) that then matures into the final conformation. Involving adjustment of side chain interactions that is relatively slow. Some proteins begin to fold as they are synthesized. For such proteins, after a domain emerges from the ribosome, it can take as little as a few seconds to form a compact structure that contains most of the final secondary structures. Some proteins require the binding of cofactors (e. g. , zn++ below), other proteins and/or covalent modifications to fold into their mature conformation.
