scholarly journals Molecular evolution of proteins on filamentous phage. Mimicking the strategy of the immune system.

1992 ◽  
Vol 267 (23) ◽  
pp. 16007-16010
Author(s):  
J.D. Marks ◽  
H.R. Hoogenboom ◽  
A.D. Griffiths ◽  
G Winter
2006 ◽  
Vol 22 (12) ◽  
pp. 662-670 ◽  
Author(s):  
P TIFFIN ◽  
D MOELLER

BioEssays ◽  
1997 ◽  
Vol 19 (9) ◽  
pp. 777-786 ◽  
Author(s):  
Austin L. Hughes ◽  
Meredith Yeager

1994 ◽  
Vol 91 (23) ◽  
pp. 10769-10770 ◽  
Author(s):  
S. Bartl ◽  
D. Baltimore ◽  
I. L. Weissman

Author(s):  
Jay F. Storz

The aims of this book are to provide a synthesis of our current understanding of hemoglobin structure, function, and evolution, and to illustrate how research on this paradigmatic protein has provided general insights into mechanisms of molecular evolution and biochemical adaptation. The book promotes an appreciation of how mechanistic insights into protein function can enrich our understanding of how evolution works and, reciprocally, it highlights how approaches in evolutionary genetics (such as phylogenetic comparative methods and ancestral sequence reconstruction) can be brought to bear on questions about the functional evolution of proteins. This treatise on the functional evolution of hemoglobin illustrates how research on a single, well-chosen model system can enhance our investigative acuity and bring key conceptual questions into sharp focus. Hemoglobin: Insights into Protein Structure, Function, and Evolution is suitable for a wide range of graduate level students taking interdisciplinary courses in biochemical physiology and protein evolution, and will serve as a key reference for researchers in molecular evolution, biochemistry, and comparative physiology.


2012 ◽  
Vol 194 (18) ◽  
pp. 5002-5011 ◽  
Author(s):  
Sujay Chattopadhyay ◽  
Sandip Paul ◽  
Dagmara I. Kisiela ◽  
Elena V. Linardopoulou ◽  
Evgeni V. Sokurenko

ABSTRACTOne of the strongest signals of adaptive molecular evolution of proteins is the occurrence of convergent hot spot mutations: repeated changes in the same amino acid positions. We performed a comparative genome-wide analysis of mutation-driven evolution of core (omnipresent) genes in 17 strains ofSalmonella entericasubspecies I and 22 strains ofEscherichia coli. More than 20% of core genes in bothSalmonellaandE. coliaccumulated hot spot mutations, with a predominance of identical changes having recent evolutionary origin. There is a significant overlap in the functional categories of the adaptively evolving genes in both species, although mostly via separate molecular mechanisms. As a strong evidence of the link between adaptive mutations and virulence inSalmonella, two human-restricted serovars, Typhi and Paratyphi A, shared the highest number of genes with serovar-specific hot spot mutations. Many of the core genes affected by Typhi/Paratyphi A-specific mutations have known virulence functions. For each species, a list of nonrecombinant core genes (and the hot spot mutations therein) under positive selection is provided.


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