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Volumn 8, Issue 12, 2013, Pages

Ligand recognition by the TPR domain of the import factor Toc64 from Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; TETRATRICOPEPTIDE REPEAT PROTEIN;

EID: 84896704985     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0083461     Document Type: Article
Times cited : (12)

References (69)
  • 1
  • 3
    • 80054856259 scopus 로고    scopus 로고
    • DARPins and other repeat protein scaffolds: Advances in engineering and applications
    • Boersma YL, Plückthun A (2011) DARPins and other repeat protein scaffolds: advances in engineering and applications. Current Opinion in Biotechnology 22: 849-857.
    • (2011) Current Opinion in Biotechnology , vol.22 , pp. 849-857
    • Boersma, Y.L.1    Plückthun, A.2
  • 4
    • 84857933257 scopus 로고    scopus 로고
    • Structural and Functional Discussion of the Tetra-Trico-Peptide Repeat, a Protein Interaction Module
    • London, England : 1993
    • Zeytuni N, Zarivach R (2012) Structural and Functional Discussion of the Tetra-Trico-Peptide Repeat, a Protein Interaction Module. Structure (London, England : 1993) 20: 397-405.
    • (2012) Structure , vol.20 , pp. 397-405
    • Zeytuni, N.1    Zarivach, R.2
  • 6
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • DOI 10.1016/S0092-8674(00)80830-2
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, et al. (2000) Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101: 199-210. (Pubitemid 32004747)
    • (2000) Cell , vol.101 , Issue.2 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl F.Ulrich7    Moarefi, I.8
  • 7
    • 80052491229 scopus 로고    scopus 로고
    • Versatile TPR domains accommodate different modes of target protein recognition and function
    • Allan RK, Ratajczak T (2011) Versatile TPR domains accommodate different modes of target protein recognition and function. Cell Stress Chaperones 16: 353-367.
    • (2011) Cell Stress Chaperones , vol.16 , pp. 353-367
    • Allan, R.K.1    Ratajczak, T.2
  • 9
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • DOI 10.1016/j.tibs.2003.10.007
    • D'Andrea LD, Regan L (2003) TPR proteins: the versatile helix. Trends in Biochemical Sciences 28: 655-662. (Pubitemid 37500900)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.12 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 10
    • 48449100534 scopus 로고    scopus 로고
    • Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5
    • Sampathkumar P, Roach C, Michels PA, Hol WG (2008) Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5. J Mol Biol 381: 867-880.
    • (2008) J Mol Biol , vol.381 , pp. 867-880
    • Sampathkumar, P.1    Roach, C.2    Michels, P.A.3    Hol, W.G.4
  • 11
    • 67649861394 scopus 로고    scopus 로고
    • IpaB-IpgC interaction defines binding motif for type III secretion translocator
    • Lunelli M, Lokareddy RK, Zychlinsky A, Kolbe M (2009) IpaB-IpgC interaction defines binding motif for type III secretion translocator. Proc Natl Acad Sci U S A 106: 9661-9666.
    • (2009) Proc Natl Acad Sci U S a , vol.106 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinsky, A.3    Kolbe, M.4
  • 12
    • 80052011286 scopus 로고    scopus 로고
    • Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly
    • Zeytuni N, Ozyamak E, Ben-Harush K, Davidov G, Levin M, et al. (2011) Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly. Proc Natl Acad Sci U S A 108: E480-487.
    • (2011) Proc Natl Acad Sci U S a , vol.108
    • Zeytuni, N.1    Ozyamak, E.2    Ben-Harush, K.3    Davidov, G.4    Levin, M.5
  • 13
    • 78149281017 scopus 로고    scopus 로고
    • The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27
    • Zhang Z, Kulkarni K, Hanrahan SJ, Thompson AJ, Barford D (2010) The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27. EMBO J 29: 3733-3744.
    • (2010) EMBO J , vol.29 , pp. 3733-3744
    • Zhang, Z.1    Kulkarni, K.2    Hanrahan, S.J.3    Thompson, A.J.4    Barford, D.5
  • 14
    • 0025122590 scopus 로고
    • The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae
    • Schultz J, Marshall-Carlson L, Carlson M (1990) The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae. Mol Cell Biol 10: 4744-4756.
    • (1990) Mol Cell Biol , vol.10 , pp. 4744-4756
    • Schultz, J.1    Marshall-Carlson, L.2    Carlson, M.3
  • 15
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski RS, Boguski MS, Goebl M, Hieter P (1990) A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 60: 307-317.
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 16
    • 0025034814 scopus 로고
    • Snap helix with knob and hole: Essential repeats in S. Pombe nuclear protein nuc2+
    • Hirano T, Kinoshita N, Morikawa K, Yanagida M (1990) Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+. Cell 60: 319-328.
    • (1990) Cell , vol.60 , pp. 319-328
    • Hirano, T.1    Kinoshita, N.2    Morikawa, K.3    Yanagida, M.4
  • 17
    • 34848823742 scopus 로고    scopus 로고
    • Mitochondrial protein-import machinery: Correlating structure with function
    • DOI 10.1016/j.tcb.2007.07.010, PII S0962892407001699
    • Baker MJ, Frazier AE, Gulbis JM, Ryan MT (2007) Mitochondrial protein-import machinery: correlating structure with function. Trends in Cell Biology 17: 456-464. (Pubitemid 47499044)
    • (2007) Trends in Cell Biology , vol.17 , Issue.9 , pp. 456-464
    • Baker, M.J.1    Frazier, A.E.2    Gulbis, J.M.3    Ryan, M.T.4
  • 18
    • 67649556148 scopus 로고    scopus 로고
    • Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria
    • Mirus O, Bionda T, Haeseler A, Schleiff E (2009) Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64 family involved in protein translocation at the outer membrane of chloroplasts and mitochondria. J Mol Model 15: 971-982.
    • (2009) J Mol Model , vol.15 , pp. 971-982
    • Mirus, O.1    Bionda, T.2    Haeseler, A.3    Schleiff, E.4
  • 19
    • 33845300838 scopus 로고    scopus 로고
    • Peroxisome targeting signal 1: Is it really a simple tripeptide?
    • DOI 10.1016/j.bbamcr.2006.08.022, PII S016748890600228X, Peroxisomes: Morphology, Function, Biogenesis and Disorders
    • Brocard C, Hartig A (2006) Peroxisome targeting signal 1: Is it really a simple tripeptide? Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1763: 1565-1573. (Pubitemid 44880463)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.12 , pp. 1565-1573
    • Brocard, C.1    Hartig, A.2
  • 20
    • 77952506871 scopus 로고    scopus 로고
    • Protein transport into chloroplasts
    • Li HM, Chiu CC (2010) Protein transport into chloroplasts. Annu Rev Plant Biol 61: 157-180.
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 157-180
    • Li, H.M.1    Chiu, C.C.2
  • 21
    • 0035997027 scopus 로고    scopus 로고
    • The chloroplast protein import channel Toc75: Pore properties and interaction with transit peptides
    • Hinnah SC, Wagner R, Sveshnikova N, Harrer R, Soll J (2002) The Chloroplast Protein Import Channel Toc75: Pore Properties and Interaction with Transit Peptides. Biophysical Journal 83: 899-911. (Pubitemid 34803623)
    • (2002) Biophysical Journal , vol.83 , Issue.2 , pp. 899-911
    • Hinnah, S.C.1    Wagner, R.2    Sveshnikova, N.3    Harrer, R.4    Soll, J.5
  • 22
    • 2442623298 scopus 로고    scopus 로고
    • atToc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins
    • DOI 10.1083/jcb.200311074
    • Smith MD, Rounds CM, Wang F, Chen K, Afitlhile M, et al. (2004) atToc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins. J Cell Biol 165: 323-334. (Pubitemid 38649908)
    • (2004) Journal of Cell Biology , vol.165 , Issue.3 , pp. 323-334
    • Smith, M.D.1    Rounds, C.M.2    Wang, F.3    Chen, K.4    Afitlhile, M.5    Schnell, D.J.6
  • 23
    • 41449086856 scopus 로고    scopus 로고
    • The GTPase Cycle of the Chloroplast Import Receptors Toc33/Toc34: Implications from Monomeric and Dimeric Structures
    • DOI 10.1016/j.str.2008.01.008, PII S0969212608000622
    • Koenig P, Oreb M, Ho? fle A, Kaltofen S, Rippe K, et al. (2008) The GTPase Cycle of the Chloroplast Import Receptors Toc33/Toc34: Implications from Monomeric and Dimeric Structures. Structure 16: 585-596. (Pubitemid 351458697)
    • (2008) Structure , vol.16 , Issue.4 , pp. 585-596
    • Koenig, P.1    Oreb, M.2    Hofle, A.3    Kaltofen, S.4    Rippe, K.5    Sinning, I.6    Schleiff, E.7    Tews, I.8
  • 24
    • 0034689055 scopus 로고    scopus 로고
    • Toc64, a new component of the protein translocon of chloroplasts
    • Sohrt K, Soll J (2000) Toc64, a new component of the protein translocon of chloroplasts. J Cell Biol 148: 1213-1221.
    • (2000) J Cell Biol , vol.148 , pp. 1213-1221
    • Sohrt, K.1    Soll, J.2
  • 26
    • 33749350156 scopus 로고    scopus 로고
    • Repeat motions and backbone flexibility in designed proteins with different numbers of identical consensus tetratricopeptide repeats
    • DOI 10.1021/bi060819a
    • Cheng CY, Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ (2006) Repeat Motions and Backbone Flexibility in Designed Proteins with Different Numbers of Identical Consensus Tetratricopeptide Repeats†. Biochemistry 45: 12175-12183. (Pubitemid 44497837)
    • (2006) Biochemistry , vol.45 , Issue.39 , pp. 12175-12183
    • Cheng, C.Y.1    Jarymowycz, V.A.2    Cortajarena, A.L.3    Regan, L.4    Stone, M.J.5
  • 27
    • 33646593202 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64
    • Qbadou S, Becker T, Mirus O, Tews I, Soll J, et al. (2006) The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J 25: 1836-1847.
    • (2006) EMBO J , vol.25 , pp. 1836-1847
    • Qbadou, S.1    Becker, T.2    Mirus, O.3    Tews, I.4    Soll, J.5
  • 28
    • 33646593202 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64
    • Qbadou S, Becker T, Mirus O, Tews I, Soll J, et al. (2006) The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64. EMBO J 25: 1836-1847.
    • (2006) EMBO J , vol.25 , pp. 1836-1847
    • Qbadou, S.1    Becker, T.2    Mirus, O.3    Tews, I.4    Soll, J.5
  • 29
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89: 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 30
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton LA, Johnson WC Jr (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal Biochem 155: 155-167. (Pubitemid 16034476)
    • (1986) Analytical Biochemistry , vol.155 , Issue.1 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 31
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan P, Johnson WC Jr (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal Biochem 167: 76-85.
    • (1987) Anal Biochem , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 32
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama N, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287: 252-260. (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Fasman GD (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8: 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 35
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding SE, Rowe AJ, Horton JC, editors. Cambridge, UK: Royal Society of Chemistry
    • Laue TM, Shah BD, Ridgeway TM, Pelletier SL (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC, editors. Analytical ultracentrifugation in biochemistry and polymer science. Cambridge, UK: Royal Society of Chemistry. pp. 90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 36
    • 83455220717 scopus 로고    scopus 로고
    • A protocol for computer-based protein structure and function prediction
    • Roy A, Xu D, Poisson J, Zhang Y (2011) A protocol for computer-based protein structure and function prediction. J Vis Exp: e3259.
    • (2011) J Vis Exp
    • Roy, A.1    Xu, D.2    Poisson, J.3    Zhang, Y.4
  • 37
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5: 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 38
    • 30344454371 scopus 로고    scopus 로고
    • Comparative modeling in CASP6 using consensus approach to template selection, sequence-structure alignment, and structure assessment
    • DOI 10.1002/prot.20725
    • Venclovas C, Margelevicius M (2005) Comparative modeling in CASP6 using consensus approach to template selection, sequence-structure alignment, and structure assessment. Proteins 61 Suppl 7: 99-105. (Pubitemid 43069962)
    • (2005) Proteins: Structure, Function and Genetics , vol.61 , Issue.SUPPL. 7 , pp. 99-105
    • Venclovas, C.1    Margelevicius, M.2
  • 39
    • 79959981040 scopus 로고    scopus 로고
    • Rosetta FlexPepDock web server-high resolution modeling of peptide-protein interactions
    • London N, Raveh B, Cohen E, Fathi G, Schueler-Furman O (2011) Rosetta FlexPepDock web server-high resolution modeling of peptide-protein interactions. Nucleic Acids Res 39: W249-253.
    • (2011) Nucleic Acids Res , vol.39
    • London, N.1    Raveh, B.2    Cohen, E.3    Fathi, G.4    Schueler-Furman, O.5
  • 40
    • 77953573815 scopus 로고    scopus 로고
    • Sub-angstrom modeling of complexes between flexible peptides and globular proteins
    • Raveh B, London N, Schueler-Furman O (2010) Sub-angstrom modeling of complexes between flexible peptides and globular proteins. Proteins 78: 2029-2040.
    • (2010) Proteins , vol.78 , pp. 2029-2040
    • Raveh, B.1    London, N.2    Schueler-Furman, O.3
  • 45
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. Journal of Computational Physics 23: 327-341.
    • (1977) Journal of Computational Physics , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 47
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • DOI 10.1006/jmbi.1994.1334
    • McDonald IK, Thornton JM (1994) Satisfying hydrogen bonding potential in proteins. Jounal of Molecular Biology 238: 777-793. (Pubitemid 24168633)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.5 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 48
    • 0004014257 scopus 로고
    • London: Department of Biochemistry and Molecular Biology University College
    • Hubbard SJ, Thornton JM (1993) NACCESS. London: Department of Biochemistry and Molecular Biology University College.
    • (1993) NACCESS
    • Hubbard, S.J.1    Thornton, J.M.2
  • 52
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8: 127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 54
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 56
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk S, Pall S, Schulz R, Larsson P, Bjelkmar P, et al. (2013) GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29: 845-854.
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1    Pall, S.2    Schulz, R.3    Larsson, P.4    Bjelkmar, P.5
  • 57
    • 33750398103 scopus 로고    scopus 로고
    • Bio3d: An R package for the comparative analysis of protein structures
    • DOI 10.1093/bioinformatics/btl461
    • Grant BJ, Rodrigues AP, ElSawy KM, McCammon JA, Caves LS (2006) Bio3d: an R package for the comparative analysis of protein structures. Bioinformatics 22: 2695-2696. (Pubitemid 44642612)
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2695-2696
    • Grant, B.J.1    Rodrigues, A.P.C.2    ElSawy, K.M.3    McCammon, J.A.4    Caves, L.S.D.5
  • 58
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M (1991) Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 11: 205-217.
    • (1991) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 62
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on position-specific scoring matrices. Jounal of Molecular Biology 292: 195-202.
    • (1999) Jounal of Molecular Biology , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 63
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • DOI 10.1110/ps.0207702
    • Lebowitz J, Lewis MS, Schuck P (2002) Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci 11: 2067-2079. (Pubitemid 34919611)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 64
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high affinity ligands
    • Campoy AV, Freire E (2006) Isothermal titration calorimetry to determine association constants for high affinity ligands. Nature Protocols 1: 186-191.
    • (2006) Nature Protocols , vol.1 , pp. 186-191
    • Campoy, A.V.1    Freire, E.2
  • 65
    • 35448962899 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: Experimental design, data analysis, probing macromolecular/ligand binding and kinetic interactions
    • Freyer MW, Lewis EA (2008) Isothermal titration calorimetry: Experimental design, data analysis, probing macromolecular/ligand binding and kinetic interactions. Methods in cell biology 84: 79-113.
    • (2008) Methods in Cell Biology , vol.84 , pp. 79-113
    • Freyer, M.W.1    Lewis, E.A.2
  • 66
    • 65249124122 scopus 로고    scopus 로고
    • Computations of standard binding free energies with molecular dynamics simulations
    • Deng Y, Roux B (2009) Computations of standard binding free energies with molecular dynamics simulations. J Phys Chem B 113: 2234-2246.
    • (2009) J Phys Chem B , vol.113 , pp. 2234-2246
    • Deng, Y.1    Roux, B.2
  • 67
    • 14944346760 scopus 로고    scopus 로고
    • Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains
    • DOI 10.1021/ja042798i
    • Krieger F, Moglich A, Kiefhaber T (2005) Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains. J Am Chem Soc 127: 3346-3352. (Pubitemid 40365272)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.10 , pp. 3346-3352
    • Krieger, F.1    Moglich, A.2    Kiefhaber, T.3
  • 68
    • 34548567337 scopus 로고    scopus 로고
    • Increasing Protein Conformational Stability by Optimizing beta-Turn Sequence
    • DOI 10.1016/j.jmb.2007.07.061, PII S0022283607010261
    • Trevino SR, Schaefer S, Scholtz JM, Pace CN (2007) Increasing protein conformational stability by optimizing beta-turn sequence. J Mol Biol 373: 211-218. (Pubitemid 47390718)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.1 , pp. 211-218
    • Trevino, S.R.1    Schaefer, S.2    Scholtz, J.M.3    Pace, C.N.4


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