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  The Magnesium Project - Proteomics

Protein Structures and Functions
(As It Relates To Cation Regulation)

Introduction to Protein Structures and Function

Proteins are organic compounds comprised of an assortment of amino acids linked together by the interaction of a carboxyl group and an amine group.  The sequence of the amino acids determines the properties of the protein. The functions of proteins a very broad ranging from providing transport vehicles across barriers and through systems and across cell membranes (as channel proteins forming pores in lipophilic membranes, serving structural components (as the endoplasmic reticulum where RNA is read as proteins are synthesized), providing mechanical forces (as in muscle proteins) and providing highly specific catalysis of most biochemical reactions (as all the enzymes).  It has been shown that the functionality of a protein is determined in part by its primary sequence (the number of type of amino acids) and in part by the secondary structure such as in a filament or global form (specifically alpha or beta helixes, sheet forms, loops, etc.) and in part by tertiary (3-dimensional form) and quaternary structures (solvent and other interactions).

Examples of different levels of structures are provided below.

  • Primary  - amino acid sequence

  • Secondary - bending and twisting

  • Tertiary - over-all 3-D shape (may include interaction with ions such as Fe, Mg, K, Ca, etc.)

  • Quaternary - interaction with solvents and other types of compounds or structures

  • Primary - FASTA formats et al.

  • Secondary - graphic vs. text

  • Tertiary  - graphic vs. x-ray crystalography

  • Quaternary

Primary & Secondary Structure/characterization of a Calcium-associated protein

Chain 1CFD:    Calmodulin

Molecular Weight           16690                                                               

Number of Residues           148                                                                   

Sequence and secondary structure

   1 ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD

          HHHHH HHHHHHHTTT TTSSSEEEHH HHTHHHHHTT     HHHHHH

  51 MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI

     HHHHHTTSSS  EEEHHHHHH HHHHHSSTT  SHHHHHHHHH HHTTTSSSEE

 101 SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

     EHHHHHHHHH HTT    HHH HHHHHHHTT  STTSEEESHH HHHHHH  

Proteins - The DSSP Code

http://www.wordiq.com/definition/Secondary_structure

The DSSP code is frequently used to describe the protein secondary structures with a single letter code. DSSP is an acronym for "Dictionary of Protein Secondary Structure", which was the title of the original article actually listing the secondary structure of the proteins with known 3D structure (Kabsch and Sander 1983). The secondary structure is assigned based on hydrogen bonding patterns as those initially proposed by Pauling et al. in 1951 (before any protein structure had ever been experimentally determined).

*                   G = 3-turn helix (3_10 helix). Min length 3 residues.

*                   H = 4-turn helix (alpha helix). Min length 4 residues.

*                   I = 5-turn helix (pi helix). Min length 5 residues.

*                   T = hydrogen bonded turn (3, 4 or 5 turn)

*                   E = beta sheet in parallel and/or anti-parallel sheet conformation (extended strand). Min length 2 residues.

*                   B = residue in isolated beta-bridge (single pair beta-sheet hydrogen bond formation)

*                   S = bend (the only non-hydrogen-bond based assignment)

In DSSP residues which are not in any of the above conformations is designated as ' ' (space), which sometimes gets designated with C (coil) or L (loop). The helices (G,H and I) and sheet conformations are all required to have a reasonable length. This means that 2 adjacent residues in the primary structure must form the same hydrogen bonding pattern. If the helix or sheet hydrogen bonding pattern is too short they are designated as T or B, respectively. Other protein secondary structure assignment categories exist (sharp turns, Omega loops etc.), but they are less frequently used.

Tertiary Structure:

Functions

  • Signaling

  • Transport

  • Enzymatic/catalysis

  • Structural

  • Transcription

  • Other

Enzymatic Roles

  • Transferase

  • Synthesis

  • Catalase

  • Nuclease

  • Phosphorylase

  • Kinase

  • Others

Transcription, Synthesis, A-A, Regulation thereof - RNA, tRNA, iRNA, miRNA etc.

Many of the proteins and enzymes indicated are involved in or require the presence of Magnesium, Calcium or other electrolytes.

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Revised: January 09, 2012

 

 

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