Interchanges of spatially neighbouring residues in structurally conserved environments

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Interchanges of spatially neighbouring residues in structurally conserved environments.

The question of whether interchanges of spatially neighboring residues are coupled, or whether they change independently of each other, has been addressed repeatedly over the last few years. Utilizing a residue order-independent structural comparison tool, we investigated interchanges of spatially adjacent residue pairs in conserved 3D environments in globally dissimilar protein structures. We ...

متن کامل

Amino acid pair interchanges at spatially conserved locations.

Here we study the pattern of amino acid interchanges at spatially, locally conserved regions in globally dissimilar and unrelated proteins. By using a method which completely separates the amino acid sequence from its respective structure, this work addresses the question of which properties of the amino acids are the most crucial for the stability of conserved structural motifs. The proteins a...

متن کامل

Identification of structurally conserved residues of proteins in absence of structural homologs using neural network ensemble

MOTIVATION So far various bioinformatics and machine learning techniques applied for identification of sequence and functionally conserved residues in proteins. Although few computational methods are available for the prediction of structurally conserved residues from protein structure, almost all methods require homologous structural information and structure-based alignments, which still prov...

متن کامل

Hot regions in protein--protein interactions: the organization and contribution of structurally conserved hot spot residues.

Structurally conserved residues at protein-protein interfaces correlate with the experimental alanine-scanning hot spots. Here, we investigate the organization of these conserved, computational hot spots and their contribution to the stability of protein associations. We find that computational hot spots are not homogeneously distributed along the protein interfaces; rather they are clustered w...

متن کامل

Align Protein Surface Structures to Identify Evolutionally and Structurally Conserved Residues∗

Protein-protein interface underlies the protein protein interaction. Alanine mutation of protein-protein interface residues has shown that the distribution of binding free energy is not average among the interface residues. Actually, there are hot spots in the protein interfaces that contribute most binding energy. Here we provide a new method based on integer quadratic programming that systema...

متن کامل

ذخیره 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: Protein Engineering Design and Selection

سال: 1997

ISSN: 1741-0126,1741-0134

DOI: 10.1093/protein/10.10.1109