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Protein Folding01:22

Protein Folding

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Protein Folding01:22

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Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Updated: Jul 11, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

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Published on: November 3, 2011

A conformational preference parameter to predict helices in integral membrane proteins.

J K Mohana Rao, P Argos

    Biochimica Et Biophysica Acta
    |January 30, 1986
    PubMed
    Summary

    This study introduces a new algorithm to identify transmembrane helices in membrane proteins, improving predictions for integral membrane protein structures.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Computational Biology

    Background:

    • Integral membrane proteins play crucial roles in cellular functions.
    • Accurate identification of transmembrane helices is essential for understanding protein structure and function.
    • Existing algorithms for helix prediction require refinement for membrane proteins.

    Purpose of the Study:

    • To develop and validate an algorithm for delineating transmembrane helices in integral membrane proteins.
    • To obtain a new conformational preference parameter specific for membrane-buried helices.
    • To analyze signal sequences and amino acid exchanges in membrane proteins.

    Main Methods:

    • An algorithm, initially developed for bacteriorhodopsin, was adapted for predicting helical regions.

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  • A novel conformational preference parameter for membrane-buried helices was derived.
  • The algorithm was applied to the L and M subunits of Rhodopseudomonas sphaeroides.

    • Main Results:

    • The algorithm successfully predicted five helices in the L and M subunits of Rhodopseudomonas sphaeroides.
    • The predictions were consistent with the known three-dimensional X-ray crystal structure.
    • Analysis of signal sequences and amino acid exchanges provided further insights.

    Conclusions:

    • The developed algorithm and new parameter enhance the prediction of transmembrane helices in integral membrane proteins.
    • This method aids in elucidating the structural organization of membrane proteins.
    • Further analysis of sequence data can refine our understanding of membrane protein biology.