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Table of Contents: July 2006

Subtle structural changes lead to distinct packing of the protein core. These changes appear due to accumulating mutations in the closely related homologous protein families. These random mutations in the ancestor protein (top) can lead to the rearrangement of the protein structure (bottom), which results in the formation of a distinct fold family (see Ding and Dokholyan).

Image Credit: Protein structures visualized with PyMOL software. Design by Nikolay V.

Reviews

From Functional Genomics to Functional Immunomics: New Challenges, Old Problems, Big Rewards

Ulisses M Braga-Neto, Ernesto T. A Marques Jr

Research Articles

Module-Based Analysis of Robustness Tradeoffs in the Heat Shock Response System

Hiroyuki Kurata, Hana El-Samad, Rei Iwasaki, Hisao Ohtake, John C Doyle, Irina Grigorova, Carol A Gross, Mustafa Khammash

Identification of Genome-Scale Metabolic Network Models Using Experimentally Measured Flux Profiles

Markus J Herrgård, Stephen S Fong, Bernhard Ø Palsson

Intronic Alternative Splicing Regulators Identified by Comparative Genomics in Nematodes

Jennifer L Kabat, Sergio Barberan-Soler, Paul McKenna, Hiram Clawson, Tracy Farrer, Alan M Zahler

Evolutionary and Physiological Importance of Hub Proteins

Nizar N Batada, Laurence D Hurst, Mike Tyers

Extracting Gene Networks for Low-Dose Radiation Using Graph Theoretical Algorithms

Brynn H Voy, Jon A Scharff, Andy D Perkins, Arnold M Saxton, Bhavesh Borate, Elissa J Chesler, Lisa K Branstetter, Michael A Langston

Wiggle—Predicting Functionally Flexible Regions from Primary Sequence

Jenny Gu, Michael Gribskov, Philip E Bourne

Toward a Census of Bacteria in Soil

Patrick D Schloss, Jo Handelsman

Complex Parameter Landscape for a Complex Neuron Model

Pablo Achard, Erik De Schutter

Circadian Rhythmicity by Autocatalysis

Arun Mehra, Christian I Hong, Mi Shi, Jennifer J Loros, Jay C Dunlap, Peter Ruoff

Correspondence

Authors' Reply

Hung D Nguyen, Maki Yoshihama, Naoya Kenmochi

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