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Related Concept Videos

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

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Peptide Bonds02:43

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Protein Organization01:24

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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End effects influence short model peptide conformation.

Liu He1, Abel E Navarro, Zhengshuang Shi

  • 1School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan 430074, PR China.

Journal of the American Chemical Society
|December 20, 2011
PubMed
Summary
This summary is machine-generated.

Peptide conformation studies reveal that the P(II) helix propensity is highly dependent on amino acid sequence and end-group modifications. This finding impacts the development of accurate peptide structure prediction models.

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Area of Science:

  • Biophysics
  • Chemical Biology
  • Structural Biology

Background:

  • Previous studies established a P(II) propensity scale for blocked peptides, suggesting P(II) as a dominant conformation.
  • Recent work on unblocked tripeptides showed differing P(II) content, highlighting potential context dependency.

Purpose of the Study:

  • To investigate the influence of pH and sequence context on P(II) helix propensity.
  • To reconcile discrepancies in P(II) propensity scales derived from different peptide models.

Main Methods:

  • Synthesis and spectroscopic analysis of three peptide series (GXG, AcGXGNH(2), AcGGXGGNH(2)) with varying amino acids (A, V, F, S).
  • pH-dependent conformational analysis using spectroscopic techniques.

Main Results:

  • P(II) content in the GXG series is pH-dependent.
  • Significant conformational differences were observed between the unblocked GXG series and the blocked AcGXGNH(2)/AcGGXGGNH(2) series.
  • Amino acid P(II) propensities are sensitive to sequence and the presence of charged end groups.

Conclusions:

  • P(II) propensity scales are not universal and are strongly influenced by peptide sequence and end-group characteristics.
  • The findings underscore the importance of considering sequence context and end-group effects in peptide structure prediction and design.