Discriminatory Power of Stoichiometry-Driven Protein Folding?
نویسندگان
چکیده
منابع مشابه
Discriminatory power of stoichiometry-driven protein folding?
There is a saying that when life hands you a lemon, you make lemonade out of it. I found that this has a parallel in molecular modeling: when your test of a putative diagnostic property fails to show discriminatory power, make an invariant out of it. The paper by Mittal, Jayaram, Shenoy and Bawa (1) is a brilliant example of this. Based on three independent observations, comparison of Cα distan...
متن کاملIs stoichiometry-driven protein folding getting out of thermodynamic control?
The views on protein folding have evolved from simple force-driven folding (3), i.e., the sum of many different small interactions (such as van der Waals interactions, hydrophobic interactions, hydrogen bonds, electrostatic interactions and ion pairs), to complex, free energy-driven “folding funnel” model (4) based on the energy landscape theory of protein folding (5). The latter is essentially...
متن کاملDoes stoichiometry drive protein folding?
Proteins are synthesized in the cell as sequential strings of amino acids. However, ribosome-emerging polypeptide chains are not active and they have to fold into a usually unique three-dimensional (3D) structure to become functional. Many proteins have been shown to attain spontaneously in vitro their native state from an initially complex ensemble of unfolded conformations in the absence of t...
متن کاملStoichiometry of amino acids drives protein folding?
Mittal et al. (1) propose that the protein folding process is a direct consequence of a narrow band of stoichiometric occurrences of amino acids in primary sequences, regardless of the size and the fold of a protein. Based on rigorous analyses of several thousand crystal structures of folded proteins, the authors suggest that “preferential interactions” between amino acids do not drive protein ...
متن کاملStoichiometry versus hydrophobicity in protein folding.
The analysis of Mittal et al. (1) is based on the counting of Ca-Ca distances in 3718 structures taken from the Protein Data Bank. Beginning with a single protein one takes an amino acid of interest (e.g., leucine). Around the Ca atom of the first leucine in the protein structure one draws a series of concentric spheres of increasing radius, X. The number of Ca atoms of any other residues that ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biomolecular Structure and Dynamics
سال: 2011
ISSN: 0739-1102,1538-0254
DOI: 10.1080/07391102.2011.10524966