Conformations of polypeptides

Ramachandran G N and Sasisekharan V 1968 Conformation of polypeptides and proteins Adv. Prof. Chem. 23 283-438... 

The lUBMB Commission on Nomenclature has issued a number of recommendations dealing with areas of a more biochemical nature (72), such as peptide hormones (86), conformation of polypeptide chains (87), abbreviations for nucleic acids and polynucleotides (88), iron—sulfur proteins (89), enzyme units (90), etc. The Commission has also produced rules and recommendations for naming enzymes (91,92). 

J Moult, MNG James. An algorithm for determining the conformation of polypeptide segments m proteins by systematic search. Proteins 1 146-163, 1986. 

Kubota S, Easman GD (1975) Beta-conformation of polypeptides of valine, isoleucine, and threonine in solution and solid-state - optical and infrared studies. Biopolymers 14 605-631... 

Ramachandran, G. N., and V. Sasisekharan. 1968. Conformation Of Polypeptides And Proteins. Adv. Protein Chem. 23, 283M38. 

Pullman, B., and A. Pullman. 1974. Molecular Orbital Calculations on the Conformation of Amino Acid Residues of Proteins, Adv. Protein Chem. 28, 347-526. Ramachandran, G. N., and V. Sasisekharan. 1968. Conformation Of Polypeptides And Proteins, Adv. Protein Chem. 23, 283—438. 

Configuration mixing model a general approach to organic reactivity, 21,99 Conformations of polypeptides, calculations of, 6,103 Conjugated molecules, reactivity indices, in, 4,73... 

Optical Rotation and the Conformation of Polypeptides and Proteins Peter Urnes and Paul Doty... 

AMINO ACIDS, PEPTIDES PROTEINS Recommended nomenclature and symbolism for amino acids and peptides J. Biol Chem. (1985) 260, 14-42 Biochemistry (1975) 14, 449-462 Abbreviations and symbols for the description of the conformation of polypeptide chains /. Biol Chem. (1970) 245, 6489-6497 Nomenclature of iron-sulfur proteins Eur. J. Biochem. (1979) 93, 427-430 Corrections Eur. J. Biochem. (1979) 102, 315 Nomenclature of peptide hormones J. Biol Chem. (1975) 250, 3215-3216 Nomenclature of human immunoglobulins Eur. J. Biochem. (1974) 45, 5-6 Recommended nomenclature of glycoproteins, glyco-peptides, and peptidoglycans /. Biol Chem. (1987) 262, 13-18 Recommended nomenclature of electron-transfer proteins... 

Miyazawa, T., In Characteristic Amide Bands and Conformations of Polypeptides, Stah-mann, M. A., Ed. University of Wisconsin Madison, WI, (1962) p 201. 

Helical fraction is the only quantity that can be estimated experimentally among the various quantities characterizing the conformation of polypeptides. There are several means of estimating helical fraction (15,16). The most commonly used is based on the assumption that the Moffitt-Yang parameter b0 derived from optical rotatory dispersion measurement is a linear function of fN. Thus... 

FIGURE 4-7 The /8 conformation of polypeptide chains. These top and side views reveal the R groups extending out from the /3 sheet and emphasize the pleated shape described by the planes of the peptide bonds. (An alternative name for this structure is /3-pleated sheet.) Hydrogen-bond cross-links between adjacent chains are also shown, (a) Antiparallel /3 sheet, in which the amino-terminal to carboxyl-terminal orientation of adjacent chains (arrows) is inverse, (b) Parallel f) sheet. 

Abbreviations and Symbols for Nucleic Adds, Polynucleotides and their Constituents http //www.chem.qmul.ac.uk/iupajc/misc7naabb.html Abbreviations and Symbols for the Description of the Conformation of Polypeptide Chains http //www.cheni.qinul.ac.uk/iiipac/misc/ppepl.hiinl Abbreviations and Symbols for the Description of Conformations of Polynucleotide Chains http //www.chem.qmul.ac.uk/iupac/misc/pnucl.htni]... 

Pauling and Corey recognized a second stable conformation of polypeptide chains —the extended chain or /3-pleated sheet (Figure 25-13). In this conformation the chains are fully extended with trans amide configurations. In this arrangement the distance is maximized between adjacent amino-acid... 

Reversible chemical oxidation reactions have also been used to control and modulate the conformation of polypeptide chains.119,101 By converting methionine to its sulfoxide, Gellman and co-workers were able to control the secondary structure of an 18-residue peptide. The side chain of a methionine residue (containing a CH2CH2SCH3 fragment) is hydrophobic and favors a-helical folding. Oxidation to the methionine sulfoxide state results in a preference for a (i-strand situation. 

Other photochromic polypeptide systems have been described, in which the ability to photocontrol the specific conformation of polypeptides is an essential feature in the design of biomaterials for devices that can be photo switched. 

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