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Structures of Proteins

Proteins are organized into the following four levels of structures [1]  [Pg.290]

The primary structure This structure is a fundamental property of a protein and describes the linear sequence of the constituent amino acids. The primary structure represents what is encoded directly by an organism s genome (the elaborate structure of DNA in a cell). In addition, this structure includes any covalent modifications of certain amino acid residues (e.g., glycosylation, phosphorylation, acylation, amidation, lipidation, and sulfation). Each class of protein in the body [Pg.290]

Threonine (Thr T) —CHCH3 Asparagine (Asn N) CH2CONH2 Glutamine (Gin Q) — CH2CH2CONH2 [Pg.291]

The tertiary structure describes how the secondary structural elements of a single protein chain interact with each other to fold into a three-dimensional conformation of protein molecules. Tertiary structures are stabilized via disulfide bridges, hydrogen bonding, salt bridges, and hydrophobic interactions. [Pg.292]

The quaternary structure determines how individual polypeptide chains (called subunits) interact to form a multimeric complex. Subunits are held together through polar and hydrophobic interactions. [Pg.292]

For convenience the structure of proteins can be considered under four basic headings. [Pg.60]

The sequence of amino acids along the polypeptide chain of a protein, as described above, is called the primary structure of the protein. [Pg.60]

The secondary structure of proteins refers to the conformation of the chain of amino acids resulting from the formation of hydrogen bonds between the imino and carbonyl groups of adjacent amino acids, as shown in Fig. 4.1. [Pg.60]

The secondary structure may be regular, in which case the polypeptide chains exist in the form of an a-helix or a P-pleated sheet, or it may be irregular and exist as, for example, a random coil. [Pg.60]

The tertiary structure describes how the chains of the secondary structure further interact through the R groups of the amino acid residues. This interaction causes folding and bending of the polypeptide chain, the specific manner of the folding giving each protein its characteristic biological activity. [Pg.60]


Plenary 2. S A Asher et al, e-mail address asher ,vms.cis.pitt.edu/asher+ (RRS, TRRRS). UV RRS is used to probe methodically the secondary structure of proteins and to follow unfolding dynamics. Developing a library based approach to generalize the mediod to any protein. [Pg.1217]

The cylinder model is used to characterize the helices in the secondary structure of proteins (see the helices in Figure 2-124c),... [Pg.134]

Chou P Y and G D Fasman 1978. Prediction of the Secondary Structure of Proteins from Tlieir Amino Acid Sequence. Advances in Enzymology 47 45-148. [Pg.574]

Mosimann S, S Meleshko and M N G Jones 1995. A Critical Assessment of Comparative Molecular Modeling of Tertiary Structures of Proteins. Proteins Structure, Function and Genetics 23 301-317. [Pg.576]

Pauling L, R B Corey and H R Bronson 1951. The Structure of Proteins Two Hydrogen-bonded He Configurations of the Polypeptide Chain. Proceedings of the National Academy of Sciences USA y . 211... [Pg.577]

Aristotle recognised the importance of water by including it among the four elements along with fire, earth and air. In its many different functions, water is essential to the earth as we know it. Life critically depends on the presence of water. It is the medium of cells and is essential for the structure of proteins, cell membranes and DNA ". It has been estimated that more than 99 % of the molecules in the human body are actually water molecules". ... [Pg.13]

The amount of computation necessary to try many conformers can be greatly reduced if a portion of the structure is known. One way to determine a portion of the structure experimentally is to obtain some of the internuclear distances from two-dimensional NMR experiments, as predicted by the nuclear Over-hauser effect (NOE). Once a set of distances are determined, they can be used as constraints within a conformation search. This has been particularly effective for predicting protein structure since it is very difficult to obtain crystallographic structures of proteins. It is also possible to define distance constraints based on the average bond lengths and angles, if we assume these are fairly rigid while all conformations are accessible. [Pg.185]

Linus Pauling (1901-1994) was born in Portland Ore gon and was educated at Oregon State University and at the California Institute of Technology where he earned a Ph D in chemistry in 1925 In addition to re search in bonding theory Pauling studied the structure of proteins and was awarded the Nobel Prize in chemistry for that work in 1954 Paul ing won a second Nobel Prize (the Peace Prize) in 1962 for his efforts to limit the testing of nuclear weapons He was one of only four scientists to have won two Nobel Prizes The first double winner was a woman Can you name her" ... [Pg.15]

This difference m reactivity especially toward hydrolysis has an important result We 11 see m Chapter 27 that the structure and function of proteins are critical to life Itself The bonds mainly responsible for the structure of proteins are amide bonds which are about 100 times more stable to hydrolysis than ester bonds These amide bonds are stable enough to maintain the structural integrity of proteins m an aqueous environment but susceptible enough to hydrolysis to be broken when the occasion demands... [Pg.834]

As m most aspects of chemistry and biochemistry structure is the key to function We 11 explore the structure of proteins by first concentrating on their fundamental building block units the a ammo acids Then after developing the principles of peptide structure we 11 see how the insights gamed from these smaller molecules aid our under standing of proteins... [Pg.1109]

Section 27 19 Two secondary structures of proteins are particularly prominent The pleated sheet is stabilized by hydrogen bonds between N—H and C=0 groups of adjacent chains The a helix is stabilized by hydrogen bonds within a single polypeptide chain... [Pg.1152]

By analogy to the levels of structure of proteins the primary structure of DNA IS the sequence of bases along the polynucleotide chain and the A DNA B DNA and Z DNA helices are varieties of secondary structures... [Pg.1169]

As the molecular structure of DNA was being elucidated, scientists made significant contributions to revealing the structures of proteins and enzymes. Sanger [2] resolved the... [Pg.1]

R Unger, D Harel, S Wherland, JL Sussman. A 3-D building blocks approach to analyzing and predicting structure of proteins. Pi otems 5 355-373, 1989. [Pg.304]

S Mosimann, R Meleshko, MNG lames. A critical assessment of comparative molecular modeling of tertiary structures of proteins. Proteins 23 301-317, 1995. [Pg.305]

B Oliva, PA Bates, E Querol, LX Aviles, MIL Sternberg. An automated classification of the structure of protein loops. I Mol Biol 266 814-830, 1997. [Pg.306]

PY Chou, CD Easman. Prediction of the secondary structure of proteins from their ammo acid sequence. Adv Enzymol Relat Areas Mol Biol 47 45-148, 1978. [Pg.347]

Chothia, C. Principles that determine the structure of proteins. Annu. Rev. Biochem. S3 537-572, 1984. [Pg.33]

Chofhia, C., Levitt, M., Richardson, D. Structure of proteins packing of a-helices and pleated sheets. [Pg.33]

Pauling, L., Corey, R.B., Branson, H.R. The structure of proteins two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sd. USA 37 205-211, 1951. [Pg.34]

Kajava, A.V., Vassart, G., Wodak, S.J. Modelling of the three-dimensional structure of proteins with the typical leucine-rich repeats. Structure 3 867-877, 1995. [Pg.64]

Cohen, F.E., Sternberg, M.J.E., Taylor, W.R. Analysis of the tertiary structure of protein p-sheet sandwiches. [Pg.87]

Several different techniques are used to study the structure of protein molecules... [Pg.373]

The three-dimensional structure of protein molecules can be experimentally determined by two different methods, x-ray crystallography and NMR. The interaction of x-rays with electrons in molecules arranged in a crystal is used to obtain an electron-density map of the molecule, which can be interpreted in terms of an atomic model. Recent technical advances, such as powerful computers including graphics work stations, electronic area detectors, and... [Pg.391]

Clore, G.M., Gronenborn, A.M. Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magetic resonance spectroscopy. CRC Crit. Rev. Biochem. 24 479-564, 1989. [Pg.392]


See other pages where Structures of Proteins is mentioned: [Pg.66]    [Pg.605]    [Pg.475]    [Pg.491]    [Pg.501]    [Pg.505]    [Pg.528]    [Pg.530]    [Pg.533]    [Pg.535]    [Pg.536]    [Pg.1110]    [Pg.2133]    [Pg.2]    [Pg.2]    [Pg.3]    [Pg.4]    [Pg.10]    [Pg.62]    [Pg.33]    [Pg.249]    [Pg.375]    [Pg.391]    [Pg.393]   
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