By Peter Tompa
"The e-book is simply great- an intensive, accomplished and lucid dialogue of intrinsically disordered proteins" --Joel L. Sussman, Weizmann Institute of Science
"Tompa's masterly compendium on Intrinsically Disordered Proteins arrives at simply the suitable time to fill a conspicuous void in this vital subject. His eminently readable publication is wide adequate to teach newcomers yet deep adequate to notify experts." -George Rose, Ph.D., Johns Hopkins collage
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Additional resources for Structure and Function of Intrinsically Disordered Proteins
Sample text
The sequence of amino acids within the polypeptide chain is defined by the succession of codons (nucleotide triplets) within the gene. Because there are four types of nucleotides in DNA, 34 = 64 different codons exist. Four of these signal for the initiation (start codon, AUG, also encoding for Met) and termination (stop codons, UAA, UAG, and UGA) of protein synthesis; thus 61 actually encode for amino acids. , the genetic code is redundant in this sense). , codons read from the 5′ end, defined by the 5′ hydroxyl group of ribose units within the backbone of DNA) toward the 3′ end of the gene correspond to amino acids, starting from the N-terminus toward the C-terminus within the protein.
Left-handed PPII helix conformation has not been recognized for a long time as an individual secondary structural element, but comprehensive studies of ordered (Adzhubei and Sternberg 1993) and intrinsically disordered (Syme et al. 2002) proteins provided evidence for the frequent occurrence of this structural element. 4C). The polypeptide chain in PPII conformation derives its stability mostly from H-bonds made with water molecules. 3) partially overlaps with the β-strand region. There are segments of proteins which cannot be described by the repetition of any of the previously described structural states, but their local conformation varies from residue to residue.
1 • Principles of Protein Structure and Function 9 of turns and the structural heterogeneity of individual residues in them, they occupy different regions in the Ramachandran plot. Left-handed PPII helix conformation has not been recognized for a long time as an individual secondary structural element, but comprehensive studies of ordered (Adzhubei and Sternberg 1993) and intrinsically disordered (Syme et al. 2002) proteins provided evidence for the frequent occurrence of this structural element.
