TITLE

Structural determinants of protein folding

AUTHOR(S)
Tse Siang Kang; Kini, R. Manjunatha
PUB. DATE
July 2009
SOURCE
Cellular & Molecular Life Sciences;Jul2009, Vol. 66 Issue 14, p2341
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The last several decades have seen an explosion of knowledge in the field of structural biology. With critical advances in spectroscopic techniques in examining structures of biomacromolecules, in maturation of molecular biology techniques, as well as vast improvements in computation prowess, protein structures are now being elucidated at an unprecedented rate. In spite of all the recent advances, the protein folding puzzle remains as one of the fundamental biochemical challenges. A facet to this empiric problem is the structural determinants of protein folding. What are the driving forces that pivot a polypeptide chain to a specific conformation amongst the vast conformation space? In this review, we shall discuss some of the structural determinants to protein folding that have been identified in the recent decades.
ACCESSION #
43029452

 

Related Articles

  • Proteins Decoded on Borrowed Time. Gravitz, Lauren // Discover;Feb2003, Vol. 24 Issue 2, p14 

    Provides information on the decoding of proteins through the Stanford project called folding@home which was used by a groupd of chemists and molecular biologists. Details of the experiment done on proteins; Significance of the research to the understanding of protein-misfolding diseases.

  • Transition states for protein folding have native topologies despite high structural variability. Lindorff-Larsen, Kresten; Vendruscolo, Michel; Paci, Emanuele; Dobson, Christopher M. // Nature Structural & Molecular Biology;May2004, Vol. 11 Issue 5, p443 

    We present a structural analysis of the folding transition states of three SH3 domains. Our results reveal that the secondary structure is not yet fully formed at this stage of folding and that the solvent is only partially excluded from the interior of the protein. Comparison of the members of...

  • Macromolecule-Assisted de novo Protein Folding. Seong Il Choi; Son, Ahyun; Keo-Heun Lim; Hotcherl Jeong; Seong, Baik L. // International Journal of Molecular Sciences;Aug2012, Vol. 13 Issue 8, p10368 

    In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo....

  • Mechanisms of protein folding. Ivarsson, Ylva; Travaglini-Allocatelli, Carlo; Brunori, Maurizio; Gianni, Stefano // European Biophysics Journal;Jul2008, Vol. 37 Issue 6, p721 

    Understanding the mechanism by which a polypeptide chain folds into its native structure is a central problem of modern biophysics. The collaborative efforts of experimental and theoretical studies recently raised the tantalizing possibility to define a unifying mechanism for protein folding. In...

  • Downhill protein folding under pressure. Muñoz, Victor // Nature Methods;Jul2009, Vol. 6 Issue 7, p490 

    The article focuses on the downhill protein folding process. It informs that in this process polypeptide chains self-assemble into specific three-dimensional structures. It states that the approach is complementary to nanosecond temperature-jump methods and could provide new insights into the...

  • Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework. England, Jeremy L.; Pande, Vijay S. // Biochemistry & Cell Biology;Apr2010, Vol. 88 Issue 2, p359 

    Water permeates all life, and mediates forces that are essential to the process of macromolecular self-assembly. Predicting these forces in a given biological context is challenging, since water organizes itself differently next to charged and hydrophobic surfaces, both of which are typically at...

  • PROTERAN: animated terrain evolution for visual analysis of patterns in protein folding trajectory. Ruhong Zhou; Laxmi Parida; Kush Kapila; Sudhir Mudur // Bioinformatics;Jan2007, Vol. 23 Issue 1, p99 

    Summary: The mechanism of protein folding remains largely a mystery in molecular biology, despite the enormous effort from many groups in the past decades. Currently, the protein folding mechanism is often characterized by calculating the free energy landscape versus various reaction coordinates...

  • Sculpting a domain by splicing. Davletov, Bazbek; Jimenez, Jose L. // Nature Structural & Molecular Biology;Jan2004, Vol. 11 Issue 1, p4 

    Comments on a study which demonstrates that a short insert from alternative splicing in a neuronal protein domain leads to rearrangements of surface loops and domain fold. Structural basis for the change of functional properties associated with alternative splicing; Functional regulation of...

  • Molecular Chaperones.  // Encyclopedic Reference of Molecular Pharmacology;2004, p602 

    The article presents an encyclopedia entry for "molecular chaperones." They refer to the protein family that mediates the correct folding of other proteins, and, in some cases, their assembly into oligomeric structures. Molecular chaperones assist the folding of protein by inhibiting the...

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics