Voronoï tessellation reveals the condensed matter character of folded proteins.
نویسندگان
چکیده
The packing geometry of amino acids in folded proteins is analyzed via a modified Voronoï tessellation method which distinguishes bulk and surface. From a statistical analysis of the Voronoï cells over 40 representative proteins, it appears that the packings are in average similar to random packings of hard spheres encountered in condensed matter physics, with a quite strong fivefold local symmetry. Moreover, the statistics permits one to establish a classification of amino acids in terms of increasing propensity to be buried in agreement with what is known from chemical considerations.
منابع مشابه
Protein secondary structure assignment through Voronoï tessellation.
We present a new automatic algorithm, named VoTAP (Voronoï Tessellation Assignment Procedure), which assigns secondary structures of a polypeptide chain using the list of alpha-carbon coordinates. This program uses three-dimensional Voronoï tessellation. This geometrical tool associates with each amino acid a Voronoï polyhedron, the faces of which unambiguously define contacts between residues....
متن کاملA Novel Vector for Expression/Secretion of Properly Folded Eukaryotic Proteins: a Comparative Study on Cytoplasmic and Periplasmic Expression of Human Epidermal Growth Factor in E. coli
Expression of eukaryotic proteins in E. coli often results in their aggregation. Proper folding and solubility of therapeutical proteins are the pre-requisite for their bioactivity. This is not achieved in cytoplasmic expression in E. coli because of the absence of disulfide bonds formation. A novel expression/secretion vector was constructed which exploited β-lactamase signal sequence to trans...
متن کاملThermodynamic character of the vibron frequencies and equation of state in dense, high-temperature, fluid N2.
متن کامل
The effect of laser pulse radiation on treatment of intra-cranial space occupying lesion (ICSOL) by the photothermal method
This article has no abstract.
متن کاملStructural bioinformatics
Motivation: Protein-protein complexes are known to play key roles in many cellular processes. However, they are often not accessible to experimental study because of their low stability and difficulty to produce the proteins and assemble them in native conformation. Thus, docking algorithms have been developed to provide an in silico approach of the problem. A protein-protein docking procedure ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Physical review letters
دوره 85 16 شماره
صفحات -
تاریخ انتشار 2000