Two possibilities exist for the evolution of individual enzymes/proteins from a milieu of amino acids, one based on preference and selectivity and the other on the basis of random events. Logic is overwhelmingly in favour of the former. By protein data base analysis and experiments, we have provided data to show the manifestation of two types of preferences, namely, the choice of the neighbour and its acceptance from the amino end (left) or the carboxyl end (right). The study tends to show that if the 20 proteinous amino acids were made to combine in water, the resulting profile would be nonrandom. Such selectivity could be a factor in protein evolution
Abstract: The autocatalytic system, N-phospho-a-amino acids, could not only self-assemble into oligo...
To investigate how the properties of individual amino acids result in proteins with particular struc...
The number of amino acids that occupy a given protein site during evolution reflects the selective c...
Key facets pertaining to the evolution of proteins have been probed, using as springboard, the relev...
The mystery of the relation between amino acid sequences and folding of the proteins started to fasc...
Local protein interactions ("molecular context" effects) dictate amino acid replacements a...
BACKGROUND: Since thermodynamic stability is a global property of proteins that has to be conserved ...
Background: Molecular evolution is a very active field of research, with several complementary appro...
Proteins are elaborate biopolymers balancing between contradicting intrinsic propensities to fold, a...
Abstract Background Since thermodynamic stability is a global property of proteins that has to be co...
Nearly all living organisms use the same set of 20 amino acids to make proteins. However, substantia...
Abstract Background Evolution at a protein site can b...
International audienceBACKGROUND: Protein-protein interactions are central to cellular organization,...
SummaryStructure propensities of amino acids are important determinants in guiding proteins' local a...
Summary. Factors involved in the selection of the 20 protein L-a-amino acids during chemical evoluti...
Abstract: The autocatalytic system, N-phospho-a-amino acids, could not only self-assemble into oligo...
To investigate how the properties of individual amino acids result in proteins with particular struc...
The number of amino acids that occupy a given protein site during evolution reflects the selective c...
Key facets pertaining to the evolution of proteins have been probed, using as springboard, the relev...
The mystery of the relation between amino acid sequences and folding of the proteins started to fasc...
Local protein interactions ("molecular context" effects) dictate amino acid replacements a...
BACKGROUND: Since thermodynamic stability is a global property of proteins that has to be conserved ...
Background: Molecular evolution is a very active field of research, with several complementary appro...
Proteins are elaborate biopolymers balancing between contradicting intrinsic propensities to fold, a...
Abstract Background Since thermodynamic stability is a global property of proteins that has to be co...
Nearly all living organisms use the same set of 20 amino acids to make proteins. However, substantia...
Abstract Background Evolution at a protein site can b...
International audienceBACKGROUND: Protein-protein interactions are central to cellular organization,...
SummaryStructure propensities of amino acids are important determinants in guiding proteins' local a...
Summary. Factors involved in the selection of the 20 protein L-a-amino acids during chemical evoluti...
Abstract: The autocatalytic system, N-phospho-a-amino acids, could not only self-assemble into oligo...
To investigate how the properties of individual amino acids result in proteins with particular struc...
The number of amino acids that occupy a given protein site during evolution reflects the selective c...