
Stephen Tsai
Professor (Research) of Aeronautics and Astronautics, Emeritus
Bio
Professor Tsai's research interest is in the development of design methodology of composite materials and structures. As an emerging technology, composite materials offer unique performances for structures that combine light weight with durability. Keys to the successful utilization of composite materials are predictability in performance and cost effective design of anisotropic, laminated structures. Current emphasis is placed on the understanding of failure modes, and computer simulation for design and cost estimation.
Academic Appointments
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Professor Emeritus-Hourly, Aeronautics and Astronautics
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Member, Cardiovascular Institute
Boards, Advisory Committees, Professional Organizations
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Member, National Academy of Engineering (1995 - Present)
2022-23 Courses
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Independent Studies (2)
- Directed Research and Writing in Aero/Astro
AA 190 (Sum) - Independent Study in Aero/Astro
AA 199 (Sum)
- Directed Research and Writing in Aero/Astro
All Publications
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Happy 40th anniversary
JOURNAL OF COMPOSITE MATERIALS
2008; 42 (18): 1821-1823
View details for DOI 10.1177/0021998308093908
View details for Web of Science ID 000258534000001
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Smart cure of thick composite filament wound structures to minimize the development of residual stresses
EUROMECH 453 Colloquium on Internal Stresses in Polymer Composite Processing and Service Life
ELSEVIER SCI LTD. 2006: 530–37
View details for DOI 10.1016/j.compositesa.2005.05.017
View details for Web of Science ID 000236338500003
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Three decades of composites activities at US Air Force Materials Laboratory
COMPOSITES SCIENCE AND TECHNOLOGY
2005; 65 (15-16): 2295-2299
View details for DOI 10.1016/j.compscitech.2005.05.017
View details for Web of Science ID 000233076100003
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Prediction of fatigue S-N curves of composite laminates by Super Mic-Mac
COMPOSITES PART A-APPLIED SCIENCE AND MANUFACTURING
2005; 36 (10): 1381-1388
View details for DOI 10.1016/j.compositesa.2004.11.016
View details for Web of Science ID 000232199000008
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Trends in the design, manufacture and evaluation of wind turbine blades
WIND ENERGY
2003; 6 (3): 245-259
View details for DOI 10.1002/we.90
View details for Web of Science ID 000186355900005
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Prediction of fatigue life for CFRP/metal bolted joint under temperature conditions
JSME/ASME International Conference on Materials and Processing
JAPAN SOC MECHANICAL ENGINEERS. 2003: 484–89
View details for Web of Science ID 000185044600052
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Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA : ACP transacylase
STRUCTURE
2003; 11 (2): 147-154
Abstract
Malonyl-CoA:ACP transacylase (MAT), the fabD gene product of Streptomyces coelicolor A3(2), participates in both fatty acid and polyketide synthesis pathways, transferring malonyl groups that are used as extender units in chain growth from malonyl-CoA to pathway-specific acyl carrier proteins (ACPs). Here, the 2.0 A structure reveals an invariant arginine bound to an acetate that mimics the malonyl carboxylate and helps define the extender unit binding site. Catalysis may only occur when the oxyanion hole is formed through substrate binding, preventing hydrolysis of the acyl-enzyme intermediate. Macromolecular docking simulations with actinorhodin ACP suggest that the majority of the ACP docking surface is formed by a helical flap. These results should help to engineer polyketide synthases (PKSs) that produce novel polyketides.
View details for Web of Science ID 000180905000006
View details for PubMedID 12575934
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Time- and temperature-dependent failures of a metal-to-composites bonded joint with PMMA adhesive material
JOURNAL OF COMPOSITE MATERIALS
2003; 37 (1): 35-54
View details for DOI 10.1106/002199803028993
View details for Web of Science ID 000180309200003
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Interlocked composite grids design and manufacturing
JOURNAL OF COMPOSITE MATERIALS
2003; 37 (4): 287-316
View details for DOI 10.1106/002199803028681
View details for Web of Science ID 000181613000001
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Expression, site-directed mutagenesis, and steady state kinetic analysis of the terminal thioesterase domain of the methymycin/picromycin polyketide synthase
BIOCHEMISTRY
2002; 41 (42): 12590-12597
Abstract
The thioesterase (TE) domain of the methymycin/picromycin synthase (PICS) was functionally expressed in Escherichia coli, and the optimal N-terminal boundary of the recombinant TE was determined. A series of diketide-N-acetylcysteamine (SNAC) thioesters were tested as substrates. PICS TE showed a strong preference for the 2-methyl-3-ketopentanoyl-SNAC substrate 5 over the stereoisomers of the reduced diketides 1-4, with an approximately 1.6:1 preference for the (2R,3S)-2-methyl-3-hydroxy diastereomer 2 over the (2S,3R)-diketide 1. The closely related DEBS TE, the thioesterase from the 6-deoxyerythronolide B synthase, showed a more marked 4.4:1 preference for 2 over 1, with only a slightly greater preference for the 3-ketoacyl-SNAC substrate 5. The roles of several active site residues in PICS TE were examined by site-directed mutagenesis. Serine 148, which is part of the apparent catalytic triad consisting of S148, H268, and D176, was found to be essential for thioesterase activity, while replacement of D176 with asparagine (D176N) gave a mutant thioesterase that retained substantial, albeit reduced, hydrolytic activity toward diketide-SNAC substrates. Mutation of E187 and R191, each of which is thought to play a role in substrate binding, had only minor effects on the relative specificity for diketide substrates 1, 2, and 5. Finally, when PICS TE was fused to the C-terminus of DEBS module 3, the resultant chimeric protein converted diketide 1 with methylmalonyl-CoA to triketide ketolactone 6 with improved catalytic efficiency compared to that of the previously developed DEBS module 3-(DEBS)TE construct.
View details for DOI 10.1021/bi026006d
View details for Web of Science ID 000178694000004
View details for PubMedID 12379101
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Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases
BIOCHEMISTRY
2002; 41 (42): 12598-12606
Abstract
Modular polyketide synthases (PKSs) synthesize the polyketide cores of pharmacologically important natural products such as erythromycin and picromycin. Understanding PKSs at high resolution could present new opportunities for chemoenzymatic synthesis of complex molecules. The crystal structures of macrocycle-forming thioesterase (TE) domains from the picromycin synthase (PICS) and 6-deoxyerythronolide B synthase (DEBS) were determined to 1.8-3.0 A with an R(crys) of 19.2-24.4%, including three structures of PICS TE (crystallized at pH 7.6, 8.0, and 8.4) and a second crystal form of DEBS TE. As predicted by the previous work on DEBS TE [Tsai, S. C., et al. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 14808-14813], PICS TE contains an open substrate channel and a hydrophobic dimer interface. Notwithstanding their similarity, the dimer interfaces and substrate channels of DEBS TE and PICS TE reveal key differences. The structural basis for the divergent substrate specificities of DEBS TE and PICS TE is analyzed. The size of the substrate channel increases with increasing pH, presumably due to electrostatic repulsion in the channel at elevated pH. Together, these structures support previous predictions that macrocycle-forming thioesterases from PKSs share the same protein fold, an open substrate channel, a similar catalytic mechanism, and a hydrophobic dimer interface. They also provide a basis for the design of enzymes capable of catalyzing regioselective macrocyclization of natural or synthetic substrates. A series of high-resolution snapshots of a protein channel at different pHs is presented alongside analysis of channel residues, which could help in the redesign of the protein channel architecture.
View details for DOI 10.1021/bi0260177
View details for Web of Science ID 000178694000005
View details for PubMedID 12379102
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Treatment of detrusor-sphincter dyssynergia by pudendal nerve block in patients with spinal cord injury
ARCHIVES OF PHYSICAL MEDICINE AND REHABILITATION
2002; 83 (5): 714-717
Abstract
To study the effects of pudendal nerve block with phenol on detrusor-sphincter dyssynergia in patients with spinal cord injury (SCI).Before-after trial performed by using a consecutive sample.Rehabilitation hospital affiliated with a medical school.Twenty-two male SCI patients (mean age, 46.3+/-11.9y; mean duration postinjury, 2.7y) with voiding dysfunction resulting from external urethral sphincter hypertonicity.Pudendal nerve block with 5% phenol solution under the guidance of electric stimulator.Outcomes were measured using (1) postvoid residual volume, maximal detrusor pressure, leak point pressure, bladder volume at the first uninhibited contraction, maximal bladder capacity, and urethral pressure profile; (2) rectoanal rest and squeeze pressures; and (3) quality of life measures for urination, quantified by the Quality of Life Index (QLI). Changes in bowel habit or autonomic dysreflexia were recorded.The mean decrease in postvoid residual volume was 242.8mL (mean decrease, 66%) after treatment (P<.001). The mean reduction in leak point pressure and maximal detrusor pressure were 37.1cmH(2)O and 43.3cmH(2)O, respectively (P<.05). The mean QLI significantly improved from -.74+/-.38 to.42+/-.47 (P<.001). The rectoanal pressures showed no significant difference. No complaints of fecal incontinence or other complications were noted after treatment.Pudendal nerve block performed by using 5% phenol solution was safe, easy to perform, and effective as a treatment for detrusor-sphincter dyssynergia in selected patients with SCI.
View details for DOI 10.1053/apmr.2002.31609
View details for Web of Science ID 000175494000019
View details for PubMedID 11994813
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A progressive quadratic failure criterion, part B
COMPOSITES SCIENCE AND TECHNOLOGY
2002; 62 (12-13): 1683-1695
View details for Web of Science ID 000177970200013
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Modeling of mechanical property degradation by short-term aging at high temperatures
COMPOSITES PART B-ENGINEERING
2002; 33 (7): 531-543
View details for Web of Science ID 000178837400004
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Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
2001; 98 (26): 14808-14813
Abstract
As the first structural elucidation of a modular polyketide synthase (PKS) domain, the crystal structure of the macrocycle-forming thioesterase (TE) domain from the 6-deoxyerythronolide B synthase (DEBS) was solved by a combination of multiple isomorphous replacement and multiwavelength anomalous dispersion and refined to an R factor of 24.1% to 2.8-A resolution. Its overall tertiary architecture belongs to the alpha/beta-hydrolase family, with two unusual features unprecedented in this family: a hydrophobic leucine-rich dimer interface and a substrate channel that passes through the entire protein. The active site triad, comprised of Asp-169, His-259, and Ser-142, is located in the middle of the substrate channel, suggesting the passage of the substrate through the protein. Modeling indicates that the active site can accommodate and orient the 6-deoxyerythronolide B precursor uniquely, while at the same time shielding the active site from external water and catalyzing cyclization by macrolactone formation. The geometry and organization of functional groups explain the observed substrate specificity of this TE and offer strategies for engineering macrocycle biosynthesis. Docking of a homology model of the upstream acyl carrier protein (ACP6) against the TE suggests that the 2-fold axis of the TE dimer may also be the axis of symmetry that determines the arrangement of domains in the entire DEBS. Sequence conservation suggests that all TEs from modular polyketide synthases have a similar fold, dimer 2-fold axis, and substrate channel geometry.
View details for Web of Science ID 000172848800016
View details for PubMedID 11752428
View details for PubMedCentralID PMC64940
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PECVD silicon carbide as a chemically resistant material for micromachined transducers
9th International Conference on Solid-State Sensors and Actuators
ELSEVIER SCIENCE SA. 1998: 48–55
View details for Web of Science ID 000075835900007
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Practical considerations for the design of composite structures
MECHANICS OF COMPOSITE MATERIALS AND STRUCTURES
1998; 5 (3): 227-255
View details for Web of Science ID 000074152200002
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A progressive quadratic failure criterion for a laminate
COMPOSITES SCIENCE AND TECHNOLOGY
1998; 58 (7): 1023-1032
View details for Web of Science ID 000076342100004
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Design optimization of composite plates: Part I - Design criteria for strength, stiffness, and manufacturing complexity of composite laminates
JOURNAL OF COMPOSITE MATERIALS
1998; 32 (6): 544-571
View details for Web of Science ID 000072859800003
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Obituary: Late Professor Tsuyoshi Hayashi
ADVANCED COMPOSITE MATERIALS
1998; 7 (3): 217-218
View details for Web of Science ID 000075585200004
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Design optimization of composite plates: Part II - Structural optimization by plydrop tapering
JOURNAL OF COMPOSITE MATERIALS
1998; 32 (6): 572-598
View details for Web of Science ID 000072859800004
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Manufacture and design of composite grids
MATERIALES DE CONSTRUCCION
1997; 47 (247-48): 59-71
View details for Web of Science ID 000071677600005
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Analysis and optimum design of composite grid structures
JOURNAL OF COMPOSITE MATERIALS
1996; 30 (4): 503-534
View details for Web of Science ID A1996UH23700005
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Analysis and behavior of grid structures
COMPOSITES SCIENCE AND TECHNOLOGY
1996; 56 (9): 1001-1015
View details for Web of Science ID A1996VR25500001
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Three-dimensional effective moduli of symmetric laminates
JOURNAL OF COMPOSITE MATERIALS
1996; 30 (8): 906-917
View details for Web of Science ID A1996UQ48000003
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SCHOOLING TAIWAN WOMEN - EDUCATIONAL-ATTAINMENT IN THE MID-20TH CENTURY
Meeting of the Research-Committee-on-Social-Stratification of the International-Sociological-Association
AMER SOCIOLOGICAL ASSOC. 1994: 243–63
View details for Web of Science ID A1994QY44300003
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3-DIMENSIONAL EFFECTIVE MODULI OF ORTHOTROPIC AND SYMMETRICAL LAMINATES
JOURNAL OF APPLIED MECHANICS-TRANSACTIONS OF THE ASME
1992; 59 (1): 39-47
View details for Web of Science ID A1992HP72000007