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Results: 1-25 | 26-26
Results: 1-25/26
A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human alpha-lactalbumin
Authors: Demarest, SJ Horng, JC Raleigh, DP
Citation: Sj. Demarest et al., A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human alpha-lactalbumin, PROTEINS, 42(2), 2001, pp. 237-242
On the relationship between protein stability and folding kinetics: A comparative study of the N-terminal domains of RNase HI, E-coli and Bacillus stearothermophilus L9
Authors: Sato, S Xiang, S Raleigh, DP
Citation: S. Sato et al., On the relationship between protein stability and folding kinetics: A comparative study of the N-terminal domains of RNase HI, E-coli and Bacillus stearothermophilus L9, J MOL BIOL, 312(3), 2001, pp. 569-577
Rescuing a destabilized protein fold through backbone cyclization
Authors: Camarero, JA Fushman, D Sato, S Giriat, I Cowburn, D Raleigh, DP Muir, TW
Citation: Ja. Camarero et al., Rescuing a destabilized protein fold through backbone cyclization, J MOL BIOL, 308(5), 2001, pp. 1045-1062
A comparative study of peptide models of the alpha-domain of alpha-lactalbumin, lysozyme, and alpha-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states
Authors: Demarest, SJ Zhou, SQ Robblee, J Fairman, R Chu, B Raleigh, DP
Citation: Sj. Demarest et al., A comparative study of peptide models of the alpha-domain of alpha-lactalbumin, lysozyme, and alpha-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states, BIOCHEM, 40(7), 2001, pp. 2138-2147
Synthesis and purification of amyloidogenic peptides
Authors: Nilsson, MR Nguyen, LL Raleigh, DP
Citation: Mr. Nilsson et al., Synthesis and purification of amyloidogenic peptides, ANALYT BIOC, 288(1), 2001, pp. 76-82
The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding
Authors: Sato, S Sayid, CJ Raleigh, DP
Citation: S. Sato et al., The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding, PROTEIN SCI, 9(8), 2000, pp. 1601-1603
Solution structure of a peptide model of a region important for the folding of alpha-lactalbumin provides evidence for the formation of nonnative structure in the denatured state
Authors: Demarest, SJ Raleigh, DP
Citation: Sj. Demarest et Dp. Raleigh, Solution structure of a peptide model of a region important for the folding of alpha-lactalbumin provides evidence for the formation of nonnative structure in the denatured state, PROTEINS, 38(2), 2000, pp. 189-196
Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state
Authors: Moriarty, DF Demarest, SJ Robblee, J Fairman, R Raleigh, DP
Citation: Df. Moriarty et al., Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state, BBA-PROT ST, 1476(1), 2000, pp. 9-19
pH-dependent interactions and the stability and folding kinetics of the n-terminal domain of L9. Electrostatic interactions are only weakly formed inthe transition state for folding
Authors: Luisi, DL Raleigh, DP
Citation: Dl. Luisi et Dp. Raleigh, pH-dependent interactions and the stability and folding kinetics of the n-terminal domain of L9. Electrostatic interactions are only weakly formed inthe transition state for folding, J MOL BIOL, 299(4), 2000, pp. 1091-1100
Rational modification of protein stability by the mutation of charged surface residues
Authors: Spector, S Wang, MH Carp, SA Robblee, J Hendsch, ZS Fairman, R Tidor, B Raleigh, DP
Citation: S. Spector et al., Rational modification of protein stability by the mutation of charged surface residues, BIOCHEM, 39(5), 2000, pp. 872-879
pH jump studies of the folding of the multidomain ribosomal protein L9: The structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain
Authors: Sato, S Luisi, DL Raleigh, DP
Citation: S. Sato et al., pH jump studies of the folding of the multidomain ribosomal protein L9: The structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain, BIOCHEM, 39(16), 2000, pp. 4955-4962
N-15 R-1 rho measurements allow the determination of ultrafast protein folding rates
Authors: Vugmeyster, L Kroenke, CD Picart, F Palmer, AG Raleigh, DP
Citation: L. Vugmeyster et al., N-15 R-1 rho measurements allow the determination of ultrafast protein folding rates, J AM CHEM S, 122(22), 2000, pp. 5387-5388
Stereospecificity of the reaction catalyzed by enoyl-CoA hydratase
Authors: Wu, WJ Feng, YG He, X Hofstein, HA Raleigh, DP Tonge, PJ
Citation: Wj. Wu et al., Stereospecificity of the reaction catalyzed by enoyl-CoA hydratase, J AM CHEM S, 122(17), 2000, pp. 3987-3994
De novo design of helical bundles as models for understanding protein folding and function
Authors: Hill, RB Raleigh, DP Lombardi, A Degrado, NF
Citation: Rb. Hill et al., De novo design of helical bundles as models for understanding protein folding and function, ACC CHEM RE, 33(11), 2000, pp. 745-754
Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin
Authors: Nilsson, MR Raleigh, DP
Citation: Mr. Nilsson et Dp. Raleigh, Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin, J MOL BIOL, 294(5), 1999, pp. 1375-1385
Defining the core structure of the alpha-lactalbumin molten globule state
Authors: Demarest, SJ Boice, JA Fairman, R Raleigh, DP
Citation: Sj. Demarest et al., Defining the core structure of the alpha-lactalbumin molten globule state, J MOL BIOL, 294(1), 1999, pp. 213-221
Submillisecond folding of the peripheral subunit-binding domain
Authors: Spector, S Raleigh, DP
Citation: S. Spector et Dp. Raleigh, Submillisecond folding of the peripheral subunit-binding domain, J MOL BIOL, 293(4), 1999, pp. 763-768
Effects of varying the local propensity to form secondary structure on thestability and folding kinetics of a rapid folding mixed alpha/beta protein: Characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9
Authors: Luisi, DL Kuhlman, B Sideras, K Evans, PA Raleigh, DP
Citation: Dl. Luisi et al., Effects of varying the local propensity to form secondary structure on thestability and folding kinetics of a rapid folding mixed alpha/beta protein: Characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9, J MOL BIOL, 289(1), 1999, pp. 167-174
Conformational analysis of a set of peptides corresponding to the entire primary sequence of the n-terminal domain of the ribosomal protein L9: Evidence for stable native-like secondary structure in the unfolded state
Authors: Luisi, DL Wu, WJ Raleigh, DP
Citation: Dl. Luisi et al., Conformational analysis of a set of peptides corresponding to the entire primary sequence of the n-terminal domain of the ribosomal protein L9: Evidence for stable native-like secondary structure in the unfolded state, J MOL BIOL, 287(2), 1999, pp. 395-407
Conformational analysis of peptide fragments derived from the peripheral subunit binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for nonrandom structure in the unfolded state
Authors: Spector, S Rosconi, M Raleigh, DP
Citation: S. Spector et al., Conformational analysis of peptide fragments derived from the peripheral subunit binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for nonrandom structure in the unfolded state, BIOPOLYMERS, 49(1), 1999, pp. 29-40
Effects of sequential proline substitutions on amyloid formation by human amylin(20-29)
Authors: Moriarty, DF Raleigh, DP
Citation: Df. Moriarty et Dp. Raleigh, Effects of sequential proline substitutions on amyloid formation by human amylin(20-29), BIOCHEM, 38(6), 1999, pp. 1811-1818
Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: A high resolution structural characterization of a peptide model in aqueous solution
Authors: Demarest, SJ Hua, YX Raleigh, DP
Citation: Sj. Demarest et al., Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: A high resolution structural characterization of a peptide model in aqueous solution, BIOCHEM, 38(22), 1999, pp. 7380-7387
Folding of the multidomain ribosomal protein L9: The two domains fold independently with remarkably different rates
Authors: Sato, S Kuhlman, B Wu, WJ Raleigh, DP
Citation: S. Sato et al., Folding of the multidomain ribosomal protein L9: The two domains fold independently with remarkably different rates, BIOCHEM, 38(17), 1999, pp. 5643-5650
pK(a) values and the pH dependent stability of the N-terminal domain of L9as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
Authors: Kuhlman, B Luisi, DL Young, P Raleigh, DP
Citation: B. Kuhlman et al., pK(a) values and the pH dependent stability of the N-terminal domain of L9as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions, BIOCHEM, 38(15), 1999, pp. 4896-4903
Nativelike structure and stability in a truncation mutant of a protein minidomain: The peripheral subunit-binding domain
Authors: Spector, S Young, P Raleigh, DP
Citation: S. Spector et al., Nativelike structure and stability in a truncation mutant of a protein minidomain: The peripheral subunit-binding domain, BIOCHEM, 38(13), 1999, pp. 4128-4136
Risultati: 1-25 | 26-26