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3 - Premixed Combustion Modeling
- Edited by N. Swaminathan, University of Cambridge, X.-S. Bai, Lunds Universitet, Sweden, N. E. L. Haugen, C. Fureby, Lunds Universitet, Sweden, G. Brethouwer, KTH Royal Institute of Technology, Stockholm
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- Book:
- Advanced Turbulent Combustion Physics and Applications
- Published online:
- 09 December 2021
- Print publication:
- 06 January 2022, pp 100-161
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4 - Drops and bubbles
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- By S. Chandra, C. T. Avedisian, M. P. Brenner, X. D. Shi, J. Eggers, S. R. Nagel, M. Tjahjadi, J. M. Ottino, PH. Marmottant, E. Villermaux, B. Vukasinovic, A. Glezer, M. K. Smith, A. Lozano, C. J. Call, C. Dopazo, D. E. Nikitopoulos, A. J. Kelly, D. Frost, B. Sturtevant, M. M. Weislogel, S. Lichter, M. Manga, H. A. Stone, J. Buchholz, L. Sigurdson, B. Peck
- M. Samimy, Ohio State University, K. S. Breuer, Brown University, Rhode Island, L. G. Leal, University of California, Santa Barbara, P. H. Steen, Cornell University, New York
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- Book:
- A Gallery of Fluid Motion
- Published online:
- 25 January 2010
- Print publication:
- 12 January 2004, pp 42-53
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Summary
The collision of a droplet with a solid surface
The photographs displayed above show the impact, spreading, and boiling history of n-heptane droplets on a stainless steel surface. The impact velocity, Weber number, and initial droplet diameter are constant (values of 1 m/s, 43 and 1.5 mm respectively), and the view is looking down on the surface at an angle of about 30°. The photographs were taken using a spark flash method and the flash duration was 0.5 μs. The dynamic behavior illustrated in the photographs is a consequence of varying the initial surface temperature.
The effect of surface temperature on droplet shape may be seen by reading across any row; the evolution of droplet shape at various temperatures may be seen by reading down any column. An entrapped air bubble can be seen in the drop when the surface temperature is 24°C. At higher temperatures vigorous bubbling, rather like that of a droplet sizzling on a frying pan, is seen (the boiling point of n-heptane is 98°C) but the bubbles disappear as the Leidenfrost temperature of n-heptane (about 200°C) is exceeded because the droplet become levitated above a cushion of its own vapor and does not make direct contact with the surface. The droplet shape is unaffected by surface temperature in the early stage of the impact process (t≤0.8 ms) but is affected by temperature at later time (cf. t≥ 1.6 ms) because of the progressive influence of intermittent solid-liquid contact as temperature is increased.
35 - The RNase A mismatch method for the genetic characterization of viruses
- Edited by Adrian J. Gibbs, Australian National University, Canberra, Charles H. Calisher, Colorado State University, Fernando García-Arenal, Universidad Politécnica de Madrid
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- Book:
- Molecular Basis of Virus Evolution
- Published online:
- 04 May 2010
- Print publication:
- 19 October 1995, pp 547-552
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Summary
Introduction and background
Point mutation has gained a lot of attention in molecular biology because of the implication of this genomic alteration in medicine and pathology, such as genetic disorders and cancers. The RNase A mismatch method was developed for the detection of point mutations related to the activation of the K-ras oncogene in colon tumours using RNA: RNA hybrids (Winter et al., 1985) and to the diagnosis of genetic disorders with RNA:DNA hybrids (Myers, Larin & Maniatis, 1985).
RNA viruses are characterized by great genetic variability. This implies the occurrence of frequent mutation in the genome of different isolates. Some of these mutations are involved in phenotypic properties, such as virulence, tropism, resistance to antiviral drugs and other characteristics (Domingo et al., 1985). They are also the basis for evolutionary studies and strain comparison. Mutations in RNA viruses have been detected by Tl oligonucleotide fingerprinting and lately by sequencing through cDNA.
Our group adapted the system of RNase A mismatch for studies on genetic variability of RNA viruses using influenza orthomyxovirus as a model (López-Galíndez et al., 1988) and Owen and Palukaitis (1988) to plant viruses. The system is based on the comparison by hybridization of a riboprobe from a reference strain with RNAs from different strains. Each one will give a complex pattern of bands resistant to the RNase A digestion which is specific for each one as a fingerprint. Comparing the different patterns we are able to draw a qualitative estimate of genetic relatedness and evolution of field strains (López-Galíndez et al., 1988, 1991).
21 - Aphthovirus evolution
- Edited by Adrian J. Gibbs, Australian National University, Canberra, Charles H. Calisher, Colorado State University, Fernando García-Arenal, Universidad Politécnica de Madrid
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- Book:
- Molecular Basis of Virus Evolution
- Published online:
- 04 May 2010
- Print publication:
- 19 October 1995, pp 310-320
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Summary
Introduction
The Aphthovirus genus, family Picornaviridae, is composed of seven distinct serotypes which cause foot-and-mouth disease (FMD), a severe disease of cloven-hoofed animals. FMD has serious economic consequences (Pereira, 1981) and is enzootic in most South American and African countries, as well as in regions of Asia and the Middle East. Foot-and-mouth disease virus (FMDV) usually causes a systemic acute infection with high morbidity and low mortality (Shanan, 1962). In ruminants, the virus may also produce an asymptomatic, persistent infection that involves limited viral amplification (Van Bekkum et al., 1959). This type of infection has been proposed as an epidemiologically important reservoir of FMDV (Hedger & Condy, 1985).
The general structure and molecular features of FMDV are, in general, similar to those of other picornaviruses (Domingo et al., 1990; Stanway, 1990). The capsid is composed of 4 proteins (VP1-4) and includes an RNA molecule of about 8500 nucleotides in length which encodes the structural proteins and at least 11 different, mature, non-structural polypeptides. The antigenic structure of FMDV includes continuous and discontinuous neutralizing epitopes located in exposed regions of the viral capsid, in which one or more of the capsid proteins, particularly VP1, are involved (Domingo et al., 1990).
Aphthoviruses show considerable antigenic diversity; 7 serotypes, more than 65 subtypes and a multitude of variants have been identified mainly by in vitro cross-serum neutralization (Pereira, 1981) and, more recently, by the use of monoclonal antibodies (MAbs) (Domingo et al., 1990). Immunization with viruses of one type does not confer protection against viruses of other serotypes, whereas cross-protection within serotypes is not always complete (Kitching et al., 1989).