Michael Pikaart/Biochem StructureIntro: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: 100px Chem311 Course Page 1 - Introduction to protein structure |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:Gata_dna.jpg|100px]] Chem311 Course Page 1 | [[Image:Gata_dna.jpg|100px]] <big>Chem311 Course Page 1 Introduction to protein structure</big> | ||
== Introduction == | |||
A protein's function depends on the proper folding of the linear polymeric chain of amino acids making up its polypeptide sequence. Folding of a polypeptide occurs by way of rotation of the single bonds in either side of each amino acid residue's alpha carbon, characterized by the Φ and Ψ angles. In folded proteins, stretches of amino acids typically have a re-iterated and restricted set of Φ and Ψ angles, giving rise to a length of stable secondary structure. If this structure has a rotational displacement, the result is a helical secondary structure; if the structure occurs in a zig-zag arrangement, a sheet secondary structure results. Here we will explore these two types of secondary structures, as found in actual proteins. | |||
== Alpha helix == | |||
Helix or screw structures are found in lots of contexts, both in nature and in man-made objects. | |||