Genonle Evolution Studied Through Protein Structure

نویسندگان

  • Philip E. Bourne
  • Kristine Briedis
  • Christopher Dupont
  • Ruben Valas
  • Song Yang
چکیده

In 1859, Charles Darwin published The Origin o/Species, a seminal work that defined the beginning of evolutionary biology (Darwin. 1859). However, Darwin's studies were con­ strained by phenotype-those characteristics of organisms that could be visibly observed, both in living and in the fossil record. The discovery of DNA as the method by which genetic information was transferred (Avery et al., 1944) and the subsequent ability to sequence DNA (Sanger and Coulson, 1975; Sanger et aI., 1977). RNA (Sanger, and later proteins (Biemann, 1992) enabled evolution to be studied at the molecular level. Advances in our evolutionary understanding came from an increase in the number of gene sequences and improved computational techniques and computational infrastructure. Combining molecular observations with observations at the species levelled to innovations such as molecular clocks (Zuckerkandl and Pauling, 1962), principles of parsimony, and to an understanding of allele frequencies based on the processes ofmutation. genetic drift, gene flow, and natural selection. Such methods have largely focused on finding similarities and differences in the DNA or protein sequences of selected organisms. As organisms evolve, events such as point

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A Study on The Effect of Temperature on Human Prion Protein Structure through Molecular Dynamic Simulation

Background & Aims: The normal form of the prion protein is called PrPC and its infectious form is called PrPSc. This protein functions like a crystallized core for the transformation of PrPc into an abnormal PrPSc. The aim of the present study was to investigate the effect of temperature on human prion protein structure through molecular dynamic simulation. Methods: In this research, the GROMAC...

متن کامل

Using the Protein-protein Interaction Network to Identifying the Biomarkers in Evolution of the Oocyte

Background Oocyte maturity includes nuclear and cytoplasmic maturity, both of which are important for embryo fertilization. The development of oocyte is not limited to the period of follicular growth, and starts from the embryonic period and continues throughout life. In this study, for the purpose of evaluating the effect of the FSH hormone on the expression of genes, GEO access codes for this...

متن کامل

Structural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c

Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...

متن کامل

Effects of T208E activating mutation on MARK2 protein structure and dynamics: Modeling and simulation

Microtubule Affinity-Regulating Kinase 2 (MARK2) protein has a substantial role in regulation of vital cellular processes like induction of polarity, regulation of cell junctions, cytoskeleton structure and cell differentiation. The abnormal function of this protein has been associated with a number of pathological conditions like Alzheimer disease, autism, several carcinomas and development of...

متن کامل

Effect of pH on Structural Properties of Heat-Induced Whey Protein Gels

Formation and structure of whey protein heat-induced gels (100 mg mL-1) through heat treatment at 80 °C and pH modifications at three pH values of acidic (2), isoelectric (5.6) and neutral (7) were studied. The obtained results indicated that the nature of the primary gel networks was different at each pH value. The heat-induced gels produced at pH of 2 and 7, had acceptab...

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

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2010