Thermal stability and protein structure

Argos, Patrick; Rossmann, Michael G.; Grau, Ulrich; Zuber, Herbert; Frank, Gerhard; Tratschin, Jon Duri

doi:10.1021/bi00592a028

Cited by 508 publications

(207 citation statements)

References 36 publications

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“…There is also no strong evidence that evolutionary changes in enzyme stability have proceeded by any particular strategy. There is a trend towards an increase in the average hydrophobicity of amino acids in some thermophilic enzymes [17] and, given that the hydrophobic effect is strongest at around 70 mC (and is weaker at temperatures above and below this), this might seem to indicate a broadly applicable stabilization strategy. However, this increase in hydrophobicity is also seen in hyperthermophilic enzymes which are stable above 100 mC [43].…”

Section: Conformational Stability At High Temperatures : Theoretical mentioning

confidence: 97%

“…Amino acid composition data were often available, sequences less frequently so, and structural information was relatively rare. On the basis of these compositional comparisons a number of fairly specific proposals were made for amino acid changes associated with increased thermal stability, for example an increased arginine\ lysine ratio [17,18]. Now enzymes that are stable over an even greater temperature range are available, and more composition (and sequence) data have been obtained, it has become apparent that these ' traffic rules ' lack predictive value and statistical significance.…”

Section: Conformational Stability Of Enzymesmentioning

confidence: 99%

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The denaturation and degradation of stable enzymes at high temperatures

Daniel

Dines

Petach³

1996

Biochemical Journal

277

175

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Now that enzymes are available that are stable above 100 mC it is possible to investigate conformational stability at this temperature, and also the effect of high-temperature degradative reactions in functioning enzymes and the inter-relationship between degradation and denaturation. The conformational stability of proteins depends upon stabilizing forces arising from a large number of weak interactions, which are opposed by an almost equally large destabilizing force due mostly to conformational entropy. The difference between these, the net free energy of stabilization, is relatively small, equivalent to a few interactions. The enhanced stability of very stable proteins can be achieved by an additional stabilizing force which is again equivalent to only a few stabilizing interactions. There is currently no strong evidence that any particular interaction (e.g. hydrogen bonds, hydrophobic interactions) plays a more important role in

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Section: Conformational Stability At High Temperatures : Theoretical mentioning

confidence: 97%

Section: Conformational Stability Of Enzymesmentioning

confidence: 99%

The denaturation and degradation of stable enzymes at high temperatures

Daniel

Dines

Petach³

1996

Biochemical Journal

277

175

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“…Arg had been proposed [9] to replace Lys in thermostable proteins based on its ability to maintain charge and provide an additional hydrogen bond. Argos [10] thought a higher Ala content in thermophilic proteins was supposed to reflect the fact that Ala was the best helix-forming residue. These Table 1 Relative single amino acid composition of all types of proteins Amino acid P ME AR P TH AR P HTH AR P HTH AR -P ME AR P ME BC P HTH BC P HTH BC -P ME BC preferences were not observed for the (hyper)thermophilic proteins we studied.…”

Section: Variation Of Single Amino Acid Compositionmentioning

confidence: 99%

The influence of dipeptide composition on protein thermostability

et al. 2004

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In this work, the influence of dipeptide composition on protein thermostability was studied. After comparing the normalized dipeptide composition between mesophilic proteins and (hyper)thermophilic proteins, we concluded that when organism optimal growth temperature increased, for archaeal proteins, the compositions of VK, KI, YK, IK, KV, KY, and EV increased significantly and the compositions of DA, AD, TD, DD, DT, HD, DH, DR, and DG decreased significantly; and for bacterial proteins, the compositions of KE, EE, EK, YE, VK, KV, KK, LK, EI, EV, RK, EF, KY, VE, KI, KG, EY, FK, KF, FE, KR, VY, MK, WK, and WE increased significantly and the compositions of WQ, AA, QA, MQ, AW, QW, QQ, RQ, QH, HQ, AD, AQ, WL, QL, HA, and DA decreased significantly. So these characteristic dipeptides are correlative to protein thermostability. At the same time, the influence of single amino acid composition on protein thermostability was also studied for comparison. We found that the influence of single amino acid composition could be deduced from the influence of dipeptide composition. So we thought that the influence of dipeptide composition on protein thermostability is larger than the influence of amino acid composition. The characteristic dipeptides not only describe the dipeptides that influence protein thermostability significantly but also show the relationship among significant single amino acids that influence protein thermostability.

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“…In addition, there is one mutation on the inside cavity of the spike facing the 5-fold axes. These mutations are mostly of the type that tend to destabilize the local protein environment 51 , thus explaining why elevated temperatures might disrupt assembly.…”

Section: Mutations Controlling Infectivity Stagesmentioning

confidence: 99%

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

McKenna

Xia

Willingmann

et al. 1992

Nature

Self Cite

217

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The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a T = 1 capsid whose major folding motif is the eightstranded antiparallel β barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight β barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome.Bacteriophage ΦX174 is a small icosahedral virus that contains a single-stranded, closed circular DNA molecule with 5,386 nucleotide bases (for a recent review, see ref. 1). Of the 11 gene products, four (J, F, G and H) participate in the structure of the virion. There are 60 copies each of the J, F and G proteins and 12 copies of the H protein per virion [2][3][4] (Table 1). Electron microscopy of shadowed or negatively stained particles [5][6][7][8] , as well as a threedimensional reconstruction of frozen-hydrated virions (Fig. 1a), clearly show large spikes at the vertices of the icosahedral particles (N.H.O., T.S.B., P.W. and N.L.I., manuscript in preparation). These spikes are about 32 Å long and have a mean diameter of 70 Å. Edgell et al. 3 have shown that these spikes, which can be removed from the capsid with 4 M urea treatment, are composed of G and H proteins. Assuming all 12 spikes are identical, then each spike will contain five G and one H protein 2 . The capsid itself has an external diameter of roughly 260 Å, with a protein shell that is about 30 Å thick, and contains the F and J proteins as well as the single-stranded (ss) DNA. The phage recognizes a lipopolysaccharide (LPS) receptor on the outer cell membrane of Escherichia coli [8][9][10][11] . Host range mutants, which determine which strains of E. coli are infected by ΦX174, map into the F, G and H genes [12][13][14][15] The infectious virion has a relative molecular mass of 6.2 × 10 6 (M r 6,200K) (26% is DNA) 32 . Lysates of infected E. coli contain two components which can be separated by sedimentation through a sucrose gradient 32,33 . The fast band contains the infectious 114S particles whereas the slow band contains noninfectious, 70S particles 32,34,35 . The latter contains about 20% of the normal DNA content with all of the genome represented in the population of particles. Both types of particles can be crystallized into isomorphous monoclinic crystals with space group P2 1 , and cell dimensions a = 305.6, b = 360.8, c = 299.5 Å, β = 92.89° that diffract at least to 2.6-Å resolution 33 . The asymmetric unit of the crystal cell contains one complete particle. We report here the three-dimensional structure...

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Thermal stability and protein structure

Cited by 508 publications

References 36 publications

The denaturation and degradation of stable enzymes at high temperatures

The denaturation and degradation of stable enzymes at high temperatures

The influence of dipeptide composition on protein thermostability

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

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