ASU Regents' Professors Open Access Works
The title “Regents’ Professor” is the highest faculty honor awarded at Arizona State University. It is conferred on ASU faculty who have made pioneering contributions in their areas of expertise, who have achieved a sustained level of distinction, and who enjoy national and international recognition for these accomplishments. This collection contains primarily open access works by ASU Regents' Professors.
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- Creators: Hunter, Mark S.
- Creators: Buman, Matthew
Description
Aim
The aim of this study was to investigate the potential associations of reallocating 30 minutes sedentary time in long bouts (>60 min) to sedentary time in non-bouts, light intensity physical activity (LPA) and moderate- to vigorous physical activity (MVPA) with cardiometabolic risk factors in a population diagnosed with prediabetes or type 2 diabetes.
Methods
Participants diagnosed with prediabetes and type 2 diabetes (n = 124, 50% men, mean [SD] age = 63.8 [7.5] years) were recruited to the physical activity intervention Sophia Step Study. For this study baseline data was used with a cross-sectional design. Time spent in sedentary behaviors in bouts (>60 min) and non-bouts (accrued in <60 min bouts) and physical activity was measured using the ActiGraph GT1M. Associations of reallocating bouted sedentary time to non-bouted sedentary time, LPA and MVPA with cardiometabolic risk factors were examined using an isotemporal substitution framework with linear regression models.
Results
Reallocating 30 minutes sedentary time in bouts to MVPA was associated with lower waist circumference (b = -4.30 95% CI:-7.23, -1.38 cm), lower BMI (b = -1.46 95% CI:-2.60, -0.33 kg/m2) and higher HDL cholesterol levels (b = 0.11 95% CI: 0.02, 0.21 kg/m[superscript 2]. Similar associations were seen for reallocation of sedentary time in non-bouts to MVPA. Reallocating sedentary time in bouts to LPA was associated only with lower waist circumference.
Conclusion
Reallocation of sedentary time in bouts as well as non-bouts to MVPA, but not to LPA, was beneficially associated with waist circumference, BMI and HDL cholesterol in individuals with prediabetes and type 2 diabetes. The results of this study confirm the importance of reallocation sedentary time to MVPA.
The aim of this study was to investigate the potential associations of reallocating 30 minutes sedentary time in long bouts (>60 min) to sedentary time in non-bouts, light intensity physical activity (LPA) and moderate- to vigorous physical activity (MVPA) with cardiometabolic risk factors in a population diagnosed with prediabetes or type 2 diabetes.
Methods
Participants diagnosed with prediabetes and type 2 diabetes (n = 124, 50% men, mean [SD] age = 63.8 [7.5] years) were recruited to the physical activity intervention Sophia Step Study. For this study baseline data was used with a cross-sectional design. Time spent in sedentary behaviors in bouts (>60 min) and non-bouts (accrued in <60 min bouts) and physical activity was measured using the ActiGraph GT1M. Associations of reallocating bouted sedentary time to non-bouted sedentary time, LPA and MVPA with cardiometabolic risk factors were examined using an isotemporal substitution framework with linear regression models.
Results
Reallocating 30 minutes sedentary time in bouts to MVPA was associated with lower waist circumference (b = -4.30 95% CI:-7.23, -1.38 cm), lower BMI (b = -1.46 95% CI:-2.60, -0.33 kg/m2) and higher HDL cholesterol levels (b = 0.11 95% CI: 0.02, 0.21 kg/m[superscript 2]. Similar associations were seen for reallocation of sedentary time in non-bouts to MVPA. Reallocating sedentary time in bouts to LPA was associated only with lower waist circumference.
Conclusion
Reallocation of sedentary time in bouts as well as non-bouts to MVPA, but not to LPA, was beneficially associated with waist circumference, BMI and HDL cholesterol in individuals with prediabetes and type 2 diabetes. The results of this study confirm the importance of reallocation sedentary time to MVPA.
ContributorsRossen, Jenny (Author) / Buman, Matthew (Author) / Johansson, Unn-Britt (Author) / Yngve, Agneta (Author) / Ainsworth, Barbara (Author) / Brismar, Kerstin (Author) / Hagstromer, Maria (Author) / College of Health Solutions (Contributor) / School of Nutrition and Health Promotion (Contributor)
Created2017-07-28
Description
X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.
ContributorsFrank, Matthias (Author) / Carlson, David B. (Author) / Hunter, Mark S. (Author) / Williams, Garth J. (Author) / Messerschmidt, Marc (Author) / Zatsepin, Nadia (Author) / Barty, Anton (Author) / Benner, W. Henry (Author) / Chu, Kaiqin (Author) / Graf, Alexander T. (Author) / Hau-Riege, Stefan P. (Author) / Kirian, Richard A. (Author) / Padeste, Celestino (Author) / Pardini, Tommaso (Author) / Pedrini, Bill (Author) / Segelke, Brent (Author) / Seibert, M. Marvin (Author) / Spence, John (Author) / Tsai, Ching-Ju (Author) / Lane, Stephen M. (Author) / Li, Xiao-Dan (Author) / Schertler, Gebhard (Author) / Boutet, Sebastien (Author) / Coleman, Matthew (Author) / Evans, James E. (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2014-02-28
Description
Serial femtosecond crystallography requires reliable and efficient delivery of fresh crystals across the beam of an X-ray free-electron laser over the course of an experiment. We introduce a double-flow focusing nozzle to meet this challenge, with significantly reduced sample consumption, while improving jet stability over previous generations of nozzles. We demonstrate its use to determine the first room-temperature structure of RNA polymerase II at high resolution, revealing new structural details. Moreover, the double flow-focusing nozzles were successfully tested with three other protein samples and the first room temperature structure of an extradiol ring-cleaving dioxygenase was solved by utilizing the improved operation and characteristics of these devices.
ContributorsOberthuer, Dominik (Author) / Knoska, Juraj (Author) / Wiedorn, Max O. (Author) / Beyerlein, Kenneth R. (Author) / Bushnell, David A. (Author) / Kovaleva, Elena G. (Author) / Heymann, Michael (Author) / Gumprecht, Lars (Author) / Kirian, Richard (Author) / Barty, Anton (Author) / Mariani, Valerio (Author) / Tolstikova, Aleksandra (Author) / Adriano, Luigi (Author) / Awel, Salah (Author) / Barthelmess, Miriam (Author) / Dorner, Katerina (Author) / Xavier, P. Lourdu (Author) / Yefanov, Oleksandr (Author) / James, Daniel (Author) / Nelson, Garrett (Author) / Wang, Dingjie (Author) / Calvey, George (Author) / Chen, Yujie (Author) / Schmidt, Andrea (Author) / Szczepek, Michael (Author) / Frielingsdorf, Stefan (Author) / Lenz, Oliver (Author) / Snell, Edward (Author) / Robinson, Philip J. (Author) / Sarler, Bozidar (Author) / Belsak, Grega (Author) / Macek, Marjan (Author) / Wilde, Fabian (Author) / Aquila, Andrew (Author) / Boutet, Sebastien (Author) / Liang, Mengning (Author) / Hunter, Mark S. (Author) / Scheerer, Patrick (Author) / Lipscomb, John D. (Author) / Weierstall, Uwe (Author) / Kornberg, Roger D. (Author) / Spence, John (Author) / Pollack, Lois (Author) / Chapman, Henry N. (Author) / Bajt, Sasa (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2017-03-16
Description
Serial femtosecond crystallography (SFX) using X-ray free-electron laser sources is an emerging method with considerable potential for time-resolved pump-probe experiments. Here we present a lipidic cubic phase SFX structure of the light-driven proton pump bacteriorhodopsin (bR) to 2.3 Å resolution and a method to investigate protein dynamics with modest sample requirement. Time-resolved SFX (TR-SFX) with a pump-probe delay of 1 ms yields difference Fourier maps compatible with the dark to M state transition of bR. Importantly, the method is very sample efficient and reduces sample consumption to about 1 mg per collected time point. Accumulation of M intermediate within the crystal lattice is confirmed by time-resolved visible absorption spectroscopy. This study provides an important step towards characterizing the complete photocycle dynamics of retinal proteins and demonstrates the feasibility of a sample efficient viscous medium jet for TR-SFX.
ContributorsNogly, Przemyslaw (Author) / Panneels, Valerie (Author) / Nelson, Garrett (Author) / Gati, Cornelius (Author) / Kimura, Tetsunari (Author) / Milne, Christopher (Author) / Milathianaki, Despina (Author) / Kubo, Minoru (Author) / Wu, Wenting (Author) / Conrad, Chelsie (Author) / Coe, Jesse (Author) / Bean, Richard (Author) / Zhao, Yun (Author) / Bath, Petra (Author) / Dods, Robert (Author) / Harimoorthy, Rajiv (Author) / Beyerlein, Kenneth R. (Author) / Rheinberger, Jan (Author) / James, Daniel (Author) / Deponte, Daniel (Author) / Li, Chufeng (Author) / Sala, Leonardo (Author) / Williams, Garth J. (Author) / Hunter, Mark S. (Author) / Koglin, Jason E. (Author) / Berntsen, Peter (Author) / Nango, Eriko (Author) / Iwata, So (Author) / Chapman, Henry N. (Author) / Fromme, Petra (Author) / Frank, Matthias (Author) / Abela, Rafael (Author) / Boutet, Sebastien (Author) / Barty, Anton (Author) / White, Thomas A. (Author) / Weierstall, Uwe (Author) / Spence, John (Author) / Neutze, Richard (Author) / Schertler, Gebhard (Author) / Standfuss, Jorg (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / Department of Chemistry and Biochemistry (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / School of Molecular Sciences (Contributor)
Created2016-08-22
Description
Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 Å resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.
ContributorsEdlund, Petra (Author) / Takala, Heikki (Author) / Claesson, Elin (Author) / Henry, Leocadie (Author) / Dods, Robert (Author) / Lehtivuori, Heli (Author) / Panman, Matthijs (Author) / Pande, Kanupriya (Author) / White, Thomas (Author) / Nakane, Takanori (Author) / Berntsson, Oskar (Author) / Gustavsson, Emil (Author) / Bath, Petra (Author) / Modi, Vaibhav (Author) / Roy Chowdhury, Shatabdi (Author) / Zook, James (Author) / Berntsen, Peter (Author) / Pandey, Suraj (Author) / Poudyal, Ishwor (Author) / Tenboer, Jason (Author) / Kupitz, Christopher (Author) / Barty, Anton (Author) / Fromme, Petra (Author) / Koralek, Jake D. (Author) / Tanaka, Tomoyuki (Author) / Spence, John (Author) / Liang, Mengning (Author) / Hunter, Mark S. (Author) / Boutet, Sebastien (Author) / Nango, Eriko (Author) / Moffat, Keith (Author) / Groenhof, Gerrit (Author) / Ihalainen, Janne (Author) / Stojkovic, Emina A. (Author) / Schmidt, Marius (Author) / Westenhoff, Sebastian (Author) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / Department of Physics (Contributor)
Created2016-10-19
Description
Serial femtosecond crystallography (SFX) has opened a new era in crystallography by permitting nearly damage-free, room-temperature structure determination of challenging proteins such as membrane proteins. In SFX, femtosecond X-ray free-electron laser pulses produce diffraction snapshots from nanocrystals and microcrystals delivered in a liquid jet, which leads to high protein consumption. A slow-moving stream of agarose has been developed as a new crystal delivery medium for SFX. It has low background scattering, is compatible with both soluble and membrane proteins, and can deliver the protein crystals at a wide range of temperatures down to 4°C. Using this crystal-laden agarose stream, the structure of a multi-subunit complex, phycocyanin, was solved to 2.5 Å resolution using 300 µg of microcrystals embedded into the agarose medium post-crystallization. The agarose delivery method reduces protein consumption by at least 100-fold and has the potential to be used for a diverse population of proteins, including membrane protein complexes.
ContributorsConrad, Chelsie (Author) / Basu, Shibom (Author) / James, Daniel (Author) / Wang, Dingjie (Author) / Schaffer, Alexander (Author) / Roy Chowdhury, Shatabdi (Author) / Zatsepin, Nadia (Author) / Aquila, Andrew (Author) / Coe, Jesse (Author) / Gati, Cornelius (Author) / Hunter, Mark S. (Author) / Koglin, Jason E. (Author) / Kupitz, Christopher (Author) / Nelson, Garrett (Author) / Subramanian, Ganesh (Author) / White, Thomas A. (Author) / Zhao, Yun (Author) / Zook, James (Author) / Boutet, Sebastien (Author) / Cherezov, Vadim (Author) / Spence, John (Author) / Fromme, Raimund (Author) / Weierstall, Uwe (Author) / Fromme, Petra (Author) / Department of Chemistry and Biochemistry (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / School of Molecular Sciences (Contributor)
Created2015-06-30
Description
Serial femtosecond crystallography (SFX) using X-ray free-electron lasers has produced high-resolution, room temperature, time-resolved protein structures. We report preliminary SFX of Sindbis virus, an enveloped icosahedral RNA virus with ∼700 Å diameter. Microcrystals delivered in viscous agarose medium diffracted to ∼40 Å resolution. Small-angle diffuse X-ray scattering overlaid Bragg peaks and analysis suggests this results from molecular transforms of individual particles. Viral proteins undergo structural changes during entry and infection, which could, in principle, be studied with SFX. This is an important step toward determining room temperature structures from virus microcrystals that may enable time-resolved studies of enveloped viruses.
ContributorsLawrence, Robert (Author) / Conrad, Chelsie (Author) / Zatsepin, Nadia (Author) / Grant, Thomas D. (Author) / Liu, Haiguang (Author) / James, Daniel (Author) / Nelson, Garrett (Author) / Subramanian, Ganesh (Author) / Aquila, Andrew (Author) / Hunter, Mark S. (Author) / Liang, Mengning (Author) / Boutet, Sebastien (Author) / Coe, Jesse (Author) / Spence, John (Author) / Weierstall, Uwe (Author) / Liu, Wei (Author) / Fromme, Petra (Author) / Cherezov, Vadim (Author) / Hogue, Brenda (Author) / Biodesign Institute (Contributor) / Infectious Diseases and Vaccinology (Contributor) / Applied Structural Discovery (Contributor) / Department of Chemistry and Biochemistry (Contributor) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / School of Life Sciences (Contributor)
Created2015-08-20
Description
Serial femtosecond crystallography (SFX) takes advantage of extremely bright and ultrashort pulses produced by x-ray free-electron lasers (XFELs), allowing for the collection of high-resolution diffraction intensities from micrometer-sized crystals at room temperature with minimal radiation damage, using the principle of “diffraction-before-destruction.” However, de novo structure factor phase determination using XFELs has been difficult so far. We demonstrate the ability to solve the crystallographic phase problem for SFX data collected with an XFEL using the anomalous signal from native sulfur atoms, leading to a bias-free room temperature structure of the human A[subscript 2A] adenosine receptor at 1.9 Å resolution. The advancement was made possible by recent improvements in SFX data analysis and the design of injectors and delivery media for streaming hydrated microcrystals. This general method should accelerate structural studies of novel difficult-to-crystallize macromolecules and their complexes.
ContributorsBatyuk, Alexander (Author) / Galli, Lorenzo (Author) / Ishchenko, Andrii (Author) / Han, Gye Won (Author) / Gati, Cornelius (Author) / Popov, Petr A. (Author) / Lee, Ming-Yue (Author) / Stauch, Benjamin (Author) / White, Thomas A. (Author) / Barty, Anton (Author) / Aquila, Andrew (Author) / Hunter, Mark S. (Author) / Liang, Mengning (Author) / Boutet, Sebastien (Author) / Pu, Mengchen (Author) / Liu, Zhi-jie (Author) / Nelson, Garrett (Author) / James, Daniel (Author) / Li, Chufeng (Author) / Zhao, Yun (Author) / Spence, John (Author) / Liu, Wei (Author) / Fromme, Petra (Author) / Katritch, Vsevolod (Author) / Weierstall, Uwe (Author) / Stevens, Raymond C. (Author) / Cherezov, Vadim (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / School of Molecular Sciences (Contributor)
Created2016-09-23
Description
Background
The purpose of this study is to determine the feasibility of three widely used wearable sensors in research settings for 24 h monitoring of sleep, sedentary, and active behaviors in middle-aged women.
Methods
Participants were 21 inactive, overweight (M Body Mass Index (BMI) = 29.27 ± 7.43) women, 30 to 64 years (M = 45.31 ± 9.67). Women were instructed to wear each sensor on the non-dominant hip (ActiGraph GT3X+), wrist (GENEActiv), or upper arm (BodyMedia SenseWear Mini) for 24 h/day and record daily wake and bed times for one week over the course of three consecutive weeks. Women received feedback about their daily physical activity and sleep behaviors. Feasibility (i.e., acceptability and demand) was measured using surveys, interviews, and wear time.
Results
Women felt the GENEActiv (94.7 %) and SenseWear Mini (90.0 %) were easier to wear and preferred the placement (68.4, 80 % respectively) as compared to the ActiGraph (42.9, 47.6 % respectively). Mean wear time on valid days was similar across sensors (ActiGraph: M = 918.8 ± 115.0 min; GENEActiv: M = 949.3 ± 86.6; SenseWear: M = 928.0 ± 101.8) and well above other studies using wake time only protocols. Informational feedback was the biggest motivator, while appearance, comfort, and inconvenience were the biggest barriers to wearing sensors. Wear time was valid on 93.9 % (ActiGraph), 100 % (GENEActiv), and 95.2 % (SenseWear) of eligible days. 61.9, 95.2, and 71.4 % of participants had seven valid days of data for the ActiGraph, GENEActiv, and SenseWear, respectively.
Conclusion
Twenty-four hour monitoring over seven consecutive days is a feasible approach in middle-aged women. Researchers should consider participant acceptability and demand, in addition to validity and reliability, when choosing a wearable sensor. More research is needed across populations and study designs.
The purpose of this study is to determine the feasibility of three widely used wearable sensors in research settings for 24 h monitoring of sleep, sedentary, and active behaviors in middle-aged women.
Methods
Participants were 21 inactive, overweight (M Body Mass Index (BMI) = 29.27 ± 7.43) women, 30 to 64 years (M = 45.31 ± 9.67). Women were instructed to wear each sensor on the non-dominant hip (ActiGraph GT3X+), wrist (GENEActiv), or upper arm (BodyMedia SenseWear Mini) for 24 h/day and record daily wake and bed times for one week over the course of three consecutive weeks. Women received feedback about their daily physical activity and sleep behaviors. Feasibility (i.e., acceptability and demand) was measured using surveys, interviews, and wear time.
Results
Women felt the GENEActiv (94.7 %) and SenseWear Mini (90.0 %) were easier to wear and preferred the placement (68.4, 80 % respectively) as compared to the ActiGraph (42.9, 47.6 % respectively). Mean wear time on valid days was similar across sensors (ActiGraph: M = 918.8 ± 115.0 min; GENEActiv: M = 949.3 ± 86.6; SenseWear: M = 928.0 ± 101.8) and well above other studies using wake time only protocols. Informational feedback was the biggest motivator, while appearance, comfort, and inconvenience were the biggest barriers to wearing sensors. Wear time was valid on 93.9 % (ActiGraph), 100 % (GENEActiv), and 95.2 % (SenseWear) of eligible days. 61.9, 95.2, and 71.4 % of participants had seven valid days of data for the ActiGraph, GENEActiv, and SenseWear, respectively.
Conclusion
Twenty-four hour monitoring over seven consecutive days is a feasible approach in middle-aged women. Researchers should consider participant acceptability and demand, in addition to validity and reliability, when choosing a wearable sensor. More research is needed across populations and study designs.
ContributorsHuberty, Jennifer (Author) / Ehlers, Diane (Author) / Kurka, Jonathan (Author) / Ainsworth, Barbara (Author) / Buman, Matthew (Author) / College of Health Solutions (Contributor) / School of Nutrition and Health Promotion (Contributor)
Created2015-07-30
Validity of the Rapid Eating Assessment for Patients for assessing dietary patterns in NCAA athletes
Description
Background
Athletes may be at risk for developing adverse health outcomes due to poor eating behaviors during college. Due to the complex nature of the diet, it is difficult to include or exclude individual food items and specific food groups from the diet. Eating behaviors may better characterize the complex interactions between individual food items and specific food groups. The purpose was to examine the Rapid Eating Assessment for Patients survey (REAP) as a valid tool for analyzing eating behaviors of NCAA Division-I male and female athletes using pattern identification. Also, to investigate the relationships between derived eating behavior patterns and body mass index (BMI) and waist circumference (WC) while stratifying by sex and aesthetic nature of the sport.
Methods
Two independent samples of male (n = 86; n = 139) and female (n = 64; n = 102) collegiate athletes completed the REAP in June-August 2011 (n = 150) and June-August 2012 (n = 241). Principal component analysis (PCA) determined possible factors using wave-1 athletes. Exploratory (EFA) and confirmatory factor analyses (CFA) determined factors accounting for error and confirmed model fit in wave-2 athletes. Wave-2 athletes' BMI and WC were recorded during a physical exam and sport participation determined classification in aesthetic and non-aesthetic sport. Mean differences in eating behavior pattern score were explored. Regression models examined interactions between pattern scores, participation in aesthetic or non-aesthetic sport, and BMI and waist circumference controlling for age and race.
Results
A 5-factor PCA solution accounting for 60.3% of sample variance determined fourteen questions for EFA and CFA. A confirmed solution revealed patterns of Desserts, Healthy food, Meats, High-fat food, and Dairy. Pattern score (mean ± SE) differences were found, as non-aesthetic sport males had a higher (better) Dessert score than aesthetic sport males (2.16 ± 0.07 vs. 1.93 ± 0.11). Female aesthetic athletes had a higher score compared to non-aesthetic female athletes for the Dessert (2.11 ± 0.11 vs. 1.88 ± 0.08), Meat (1.95 ± 0.10 vs. 1.72 ± 0.07), High-fat food (1.70 ± 0.08 vs. 1.46 ± 0.06), and Dairy (1.70 ± 0.11 vs. 1.43 ± 0.07) patterns.
Conclusions
REAP is a construct valid tool to assess dietary patterns in college athletes. In light of varying dietary patterns, college athletes should be evaluated for healthful and unhealthful eating behaviors.
Athletes may be at risk for developing adverse health outcomes due to poor eating behaviors during college. Due to the complex nature of the diet, it is difficult to include or exclude individual food items and specific food groups from the diet. Eating behaviors may better characterize the complex interactions between individual food items and specific food groups. The purpose was to examine the Rapid Eating Assessment for Patients survey (REAP) as a valid tool for analyzing eating behaviors of NCAA Division-I male and female athletes using pattern identification. Also, to investigate the relationships between derived eating behavior patterns and body mass index (BMI) and waist circumference (WC) while stratifying by sex and aesthetic nature of the sport.
Methods
Two independent samples of male (n = 86; n = 139) and female (n = 64; n = 102) collegiate athletes completed the REAP in June-August 2011 (n = 150) and June-August 2012 (n = 241). Principal component analysis (PCA) determined possible factors using wave-1 athletes. Exploratory (EFA) and confirmatory factor analyses (CFA) determined factors accounting for error and confirmed model fit in wave-2 athletes. Wave-2 athletes' BMI and WC were recorded during a physical exam and sport participation determined classification in aesthetic and non-aesthetic sport. Mean differences in eating behavior pattern score were explored. Regression models examined interactions between pattern scores, participation in aesthetic or non-aesthetic sport, and BMI and waist circumference controlling for age and race.
Results
A 5-factor PCA solution accounting for 60.3% of sample variance determined fourteen questions for EFA and CFA. A confirmed solution revealed patterns of Desserts, Healthy food, Meats, High-fat food, and Dairy. Pattern score (mean ± SE) differences were found, as non-aesthetic sport males had a higher (better) Dessert score than aesthetic sport males (2.16 ± 0.07 vs. 1.93 ± 0.11). Female aesthetic athletes had a higher score compared to non-aesthetic female athletes for the Dessert (2.11 ± 0.11 vs. 1.88 ± 0.08), Meat (1.95 ± 0.10 vs. 1.72 ± 0.07), High-fat food (1.70 ± 0.08 vs. 1.46 ± 0.06), and Dairy (1.70 ± 0.11 vs. 1.43 ± 0.07) patterns.
Conclusions
REAP is a construct valid tool to assess dietary patterns in college athletes. In light of varying dietary patterns, college athletes should be evaluated for healthful and unhealthful eating behaviors.
ContributorsKurka, Jonathan (Author) / Buman, Matthew (Author) / Ainsworth, Barbara (Author) / College of Health Solutions (Contributor) / School of Nutrition and Health Promotion (Contributor)
Created2014-08-15