Classes of globular proteins: Difference between revisions

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Globular proteins have a molecular structure that has the  appearance of a glob whose 3D structure is anywhere from a sphere to a cigar.  Usually the structure of a globular protein is divided into three or four levels.  The primary structure is simply the sequence of amino acids forming the peptide chain.  The peptide chain is folded in a repetitive fashion, and these structures with repetitive conformations are called [[Secondary_structure|secondary structures]].  Common examples of secondary structures are [[Helices_in_Proteins|α-helix]] and β-sheets.  The tertiary structure is the overall 3D structure of a protein molecule and is produced by folding the secondary structures upon themselves, and in the process the sections of the peptide that were not involved in secondary structures form turns (tight loops) and loops.  Some globular proteins have a quaternary structure, and it is formed when two or more globular protein molecules (monomer) join together and form a multimeric unit.  One way of characterizing globular proteins is by the number of layers of backbones the tertiary structures contain.  A convenient way of classifying globular proteins is to categorize them according to the type and arrangement of secondary structures that are present and the intramolecular forces that are produced by these arrangements.  A study of these characteristics and classes using specific examples will be presented in this page.


Globular proteins have a molecular structure that has the  appearance of a glob whose 3D structure is anywhere from a sphere to a cigar.  Usually the structure of a globular protein is divided into three or four levels.  The primary structure is simply the sequence of amino acids forming the peptide chain.  The peptide chain is folded in a repetitive fashion, and these structures with repetitive conformations are called [[Secondary_structure|secondary structures]].  Common examples of secondary structures are [[Helices_in_Proteins|α-helix]] and β-sheets.  The tertiary structure is the overall 3D structure of a protein molecule and is produced by folding the secondary structures upon themselves, and in the process the sections of the peptide that were not involved in secondary structures form turns (tight loops) and loops.  One way of characterizing globular proteins is by the number of layers of backbones the protein contains.  A convenient way of classifying globular proteins is to categorize them according to the type and arrangement of secondary structures that are present, as well as the important forces that maintain the globular structure. A study of the different classes using specific examples with Jmol is found [http://www.messiah.edu/molscilab/my_molecules/molslides/my_slides/jmol-10.2.0/Classes%20globular.htm#1 here].
== Layers of Backbone Present in the Structure ==
In the process of folding
 
Layers of backbone in the core of the structure is a feature that many, but not all, globular proteins have. The number of layers and their composition vary for different proteins, but in all case the hydrophobic forces between the layers play a major role in maintaining the tertiary structure.
 
<table width='500' align='right' cellpadding='5'><tr><td rowspan='2'>&nbsp;</td><td bgcolor='#eeeeee'><applet load='1a7v' size='490' frame='true' align='right' scene ='Classes_of_globular_proteins/Two_layers/2' caption='' /></td></tr><tr><td bgcolor='#eeeeee'><center>'''Tertiary Structures of Examples'''<scene name='Classes_of_globular_proteins/Two_layers/2'> (Initial scene)</scene></center></td></tr></table>
 
=== Two Layers ===
The ribbons representing the backbones show the two layers of α-helices.

Revision as of 21:36, 4 February 2011

Globular proteins have a molecular structure that has the appearance of a glob whose 3D structure is anywhere from a sphere to a cigar. Usually the structure of a globular protein is divided into three or four levels. The primary structure is simply the sequence of amino acids forming the peptide chain. The peptide chain is folded in a repetitive fashion, and these structures with repetitive conformations are called secondary structures. Common examples of secondary structures are α-helix and β-sheets. The tertiary structure is the overall 3D structure of a protein molecule and is produced by folding the secondary structures upon themselves, and in the process the sections of the peptide that were not involved in secondary structures form turns (tight loops) and loops. Some globular proteins have a quaternary structure, and it is formed when two or more globular protein molecules (monomer) join together and form a multimeric unit. One way of characterizing globular proteins is by the number of layers of backbones the tertiary structures contain. A convenient way of classifying globular proteins is to categorize them according to the type and arrangement of secondary structures that are present and the intramolecular forces that are produced by these arrangements. A study of these characteristics and classes using specific examples will be presented in this page.

Layers of Backbone Present in the StructureLayers of Backbone Present in the Structure

Layers of backbone in the core of the structure is a feature that many, but not all, globular proteins have. The number of layers and their composition vary for different proteins, but in all case the hydrophobic forces between the layers play a major role in maintaining the tertiary structure.

 

PDB ID 1a7v

Drag the structure with the mouse to rotate
Tertiary Structures of Examples

Two LayersTwo Layers

The ribbons representing the backbones show the two layers of α-helices.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Karl Oberholser, Eric Martz