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Volumn 18, Issue 9, 2009, Pages 1967-1977

Stereoelectronic effects on the transition barrier of polyproline conformational interconversion

Author keywords

Fluoroproline; Host guest peptide; Hydroxyproline; Methoxyproline; Polyproline; Stereoelectronic effect; Transition state barrier

Indexed keywords

4 FLUOROPROLINE; HYDROXYPROLINE; METHOXYPROLINE; POLYPROLINE; PROLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 69249155999     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.208     Document Type: Article
Times cited : (50)

References (37)
  • 1
    • 12944281484 scopus 로고    scopus 로고
    • On the stability of polyproline-I and II structures of proline oligopeptides
    • Kakinoki S, Hirano Y, Oka M (2005) On the stability of polyproline-I and II structures of proline oligopeptides. Polym Bull 53:109-115.
    • (2005) Polym Bull , vol.53 , pp. 109-115
    • Kakinoki, S.1    Hirano, Y.2    Oka, M.3
  • 2
    • 84987344516 scopus 로고
    • Conformational stability, partial specific volumes and spectroscopic properties of poly-L-proline, poly-L-hydroxyproline and some of its O-acyl-derivatives in various solvent systems
    • Knof S, Engel J (1974) Conformational stability, partial specific volumes and spectroscopic properties of poly-L-proline, poly-L-hydroxyproline and some of its O-acyl-derivatives in various solvent systems. Isr J Chem 12:165-177.
    • (1974) Isr J Chem , vol.12 , pp. 165-177
    • Knof, S.1    Engel, J.2
  • 3
    • 0032801691 scopus 로고    scopus 로고
    • Pseudoprolines: Induction of cis/trans-conformational interconversion by decreased transition state barriers
    • Mutter M, Wohr T, Gioria S, Keller M (1999) Pseudoprolines: induction of cis/trans-conformational interconversion by decreased transition state barriers. Biopolymers 51:121-128.
    • (1999) Biopolymers , vol.51 , pp. 121-128
    • Mutter, M.1    Wohr, T.2    Gioria, S.3    Keller, M.4
  • 4
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio B, Tamburro AM (2002) Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions. Chirality 14:782-792.
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 5
    • 0038656707 scopus 로고    scopus 로고
    • NMR identification of left-handed polyproline type II helices
    • Lam SL, Hsu VL (2003) NMR identification of left-handed polyproline type II helices. Biopolymers 69:270-281.
    • (2003) Biopolymers , vol.69 , pp. 270-281
    • Lam, S.L.1    Hsu, V.L.2
  • 6
    • 2942712684 scopus 로고    scopus 로고
    • Thermodynamic mechanism and consequences of the polyproline II (P-II) structural bias in the denatured states of proteins
    • Hamburger JB, Ferreon JC, Whitten ST, Hilser VJ (2004) Thermodynamic mechanism and consequences of the polyproline II (P-II) structural bias in the denatured states of proteins. Biochemistry 43:9790-9799.
    • (2004) Biochemistry , vol.43 , pp. 9790-9799
    • Hamburger, J.B.1    Ferreon, J.C.2    Whitten, S.T.3    Hilser, V.J.4
  • 7
    • 17644422781 scopus 로고    scopus 로고
    • Urea promotes polyproline II helix formation: Implications for protein denatured states
    • Whittington SJ, Chellgren BW, Hermann VM, Creamer TP (2005) Urea promotes polyproline II helix formation: implications for protein denatured states. Biochemistry 44:6269-6275.
    • (2005) Biochemistry , vol.44 , pp. 6269-6275
    • Whittington, S.J.1    Chellgren, B.W.2    Hermann, V.M.3    Creamer, T.P.4
  • 8
    • 33646908786 scopus 로고    scopus 로고
    • Conformation of the backbone in unfolded proteins
    • Shi ZS, Chen K, Liu ZG, Kallenbach NR (2006) Conformation of the backbone in unfolded proteins. Chem Rev 106:1877-1897.
    • (2006) Chem Rev , vol.106 , pp. 1877-1897
    • Shi, Z.S.1    Chen, K.2    Liu, Z.G.3    Kallenbach, N.R.4
  • 9
    • 0027474991 scopus 로고
    • Left-handed polyproline-II helices commonly occur in globular-proteins
    • Adzhubei AA, Sternberg MJE (1993) Left-handed polyproline-II helices commonly occur in globular-proteins. J Mol Biol 229:472-493.
    • (1993) J Mol Biol , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 10
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisited
    • Kleywegt GJ, Jones TA (1996) Phi/Psi-chology: Ramachandran revisited. Structure 4:1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 11
    • 0029058133 scopus 로고
    • The importance of extended conformtions and, in particular, the PII conformation for the molecular recognition of peptides
    • Siligardi G, Drake AF (1995) The importance of extended conformtions and, in particular, the PII conformation for the molecular recognition of peptides. Biopolymers 37:281-292.
    • (1995) Biopolymers , vol.37 , pp. 281-292
    • Siligardi, G.1    Drake, A.F.2
  • 12
  • 13
    • 0015850668 scopus 로고
    • Role of a rigid polyproline space inserted between hapten and carrier in induction of anti-hapten antibodies and delayed hypersensitivity
    • Ungar-waron H, Gurari D, Hurwitz E, Sela M (1973) Role of a rigid polyproline space inserted between hapten and carrier in induction of anti-hapten antibodies and delayed hypersensitivity. Eur J Immunol 3:201-205.
    • (1973) Eur J Immunol , vol.3 , pp. 201-205
    • Ungar-waron, H.1    Gurari, D.2    Hurwitz, E.3    Sela, M.4
  • 14
    • 33846681655 scopus 로고    scopus 로고
    • Polyproline-rod approach to isolating protein targets of bioactive small molecules: Isolation of a new target of indomethacin
    • Sato S, Kwon Y, Kamisuki S, Srivastava N, Mao QA, Kawazoe Y, Uesugi M (2007) Polyproline-rod approach to isolating protein targets of bioactive small molecules: isolation of a new target of indomethacin. J Am Chem Soc 129:873-880.
    • (2007) J Am Chem Soc , vol.129 , pp. 873-880
    • Sato, S.1    Kwon, Y.2    Kamisuki, S.3    Srivastava, N.4    Mao, Q.A.5    Kawazoe, Y.6    Uesugi, M.7
  • 15
    • 23944492106 scopus 로고    scopus 로고
    • Cell penetrating agents based on a polyproline helix scaffold
    • Fillon YA, Anderson JP, Chmielewski J (2005) Cell penetrating agents based on a polyproline helix scaffold. J Am Chem Soc 127:11798-11803.
    • (2005) J Am Chem Soc , vol.127 , pp. 11798-11803
    • Fillon, Y.A.1    Anderson, J.P.2    Chmielewski, J.3
  • 16
    • 34247382518 scopus 로고    scopus 로고
    • Probing length effects and mechanism of cell penetrating agents mounted on a polyproline helix scaffold
    • Geisler I, Chmielewski J (2007) Probing length effects and mechanism of cell penetrating agents mounted on a polyproline helix scaffold. Bioorg Med Chem Lett 17:2765-2768.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 2765-2768
    • Geisler, I.1    Chmielewski, J.2
  • 18
    • 2442522724 scopus 로고    scopus 로고
    • Short sequences of non-proline residues can adopt the polyproline II helical conformation
    • Chellgren BW, Creamer TP (2004) Short sequences of non-proline residues can adopt the polyproline II helical conformation. Biochemistry 43:5864-5869.
    • (2004) Biochemistry , vol.43 , pp. 5864-5869
    • Chellgren, B.W.1    Creamer, T.P.2
  • 19
    • 0002251831 scopus 로고
    • Circular dichroism and conformation of unordered polypeptides
    • Woody RW (1992) Circular dichroism and conformation of unordered polypeptides. Adv Biophys Chem 2:37-79.
    • (1992) Adv Biophys Chem , vol.2 , pp. 37-79
    • Woody, R.W.1
  • 20
    • 0038344087 scopus 로고    scopus 로고
    • Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy
    • Eker F, Griebenow K, Schweitzer-Stenner R (2003) Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy. J Am Chem Soc 125:8178-8185.
    • (2003) J Am Chem Soc , vol.125 , pp. 8178-8185
    • Eker, F.1    Griebenow, K.2    Schweitzer-Stenner, R.3
  • 21
    • 13944275600 scopus 로고    scopus 로고
    • Properties of polyproline II, a secondary structure element implicated in protein-protein interactions
    • Cubellis MV, Caillez F, Blundell TL, Lovell SC (2005) Properties of polyproline II, a secondary structure element implicated in protein-protein interactions. Proteins 58:880-892.
    • (2005) Proteins , vol.58 , pp. 880-892
    • Cubellis, M.V.1    Caillez, F.2    Blundell, T.L.3    Lovell, S.C.4
  • 24
    • 0036402323 scopus 로고    scopus 로고
    • Determinants of the polyproline II helix from modeling studies
    • Creamer TP, Campbell MN (2002) Determinants of the polyproline II helix from modeling studies. Adv Protein Chem 62:263-282.
    • (2002) Adv Protein Chem , vol.62 , pp. 263-282
    • Creamer, T.P.1    Campbell, M.N.2
  • 25
    • 0036129072 scopus 로고    scopus 로고
    • Polyproline II helical structure in protein unfolded states: Lysine peptides revisited
    • Rucker AL, Creamer TP (2002) Polyproline II helical structure in protein unfolded states: lysine peptides revisited. Protein Sci 11:980-985.
    • (2002) Protein Sci , vol.11 , pp. 980-985
    • Rucker, A.L.1    Creamer, T.P.2
  • 27
    • 0038245117 scopus 로고    scopus 로고
    • An electronic effect on protein structure
    • Hinderaker MP, Raines RT (2003) An electronic effect on protein structure. Protein Sci 12:1188-1194.
    • (2003) Protein Sci , vol.12 , pp. 1188-1194
    • Hinderaker, M.P.1    Raines, R.T.2
  • 28
    • 33750361975 scopus 로고    scopus 로고
    • Energetics of an n → π* interaction that impacts protein structure
    • Hodges JA, Raines RT (2006) Energetics of an n → π* interaction that impacts protein structure. Org Lett 8:4695-4697.
    • (2006) Org Lett , vol.8 , pp. 4695-4697
    • Hodges, J.A.1    Raines, R.T.2
  • 29
    • 29344463669 scopus 로고    scopus 로고
    • Stereoelectronic effects on polyproline conformation
    • Horng JC, Raines RT (2006) Stereoelectronic effects on polyproline conformation. Protein Sci 15:74-83.
    • (2006) Protein Sci , vol.15 , pp. 74-83
    • Horng, J.C.1    Raines, R.T.2
  • 30
    • 42949115809 scopus 로고    scopus 로고
    • The effect of a trans-locked Gly-Pro alkene isostere on collagen triple helix stability
    • Dai N, Wang XJ, Etzkorn FA (2008) The effect of a trans-locked Gly-Pro alkene isostere on collagen triple helix stability. J Am Chem Soc 130:5396-5397.
    • (2008) J Am Chem Soc , vol.130 , pp. 5396-5397
    • Dai, N.1    Wang, X.J.2    Etzkorn, F.A.3
  • 31
    • 33846415089 scopus 로고    scopus 로고
    • Azidoproline containing helices: Stabilization of the polyproline II structure by a functionalizable group
    • Kümin M, Sonntag LS, Wennemers H (2007) Azidoproline containing helices: stabilization of the polyproline II structure by a functionalizable group. J Am Chem Soc 129:466-467.
    • (2007) J Am Chem Soc , vol.129 , pp. 466-467
    • Kümin, M.1    Sonntag, L.S.2    Wennemers, H.3
  • 32
    • 44349123059 scopus 로고    scopus 로고
    • Toward quantification of protein backbone-backbone hydrogen bonding energies: An energetic analysis of an amide-to-ester mutation in an alpha-helix within a protein
    • Gao J, Kelly JW (2008) Toward quantification of protein backbone-backbone hydrogen bonding energies: an energetic analysis of an amide-to-ester mutation in an alpha-helix within a protein. Protein Sci 17:1096-1101.
    • (2008) Protein Sci , vol.17 , pp. 1096-1101
    • Gao, J.1    Kelly, J.W.2
  • 33
    • 34547491911 scopus 로고    scopus 로고
    • Local and tunable n→π* interactions regulate amide isomerism in the peptoid backbone
    • Gorske BC, Bastian BL, Geske GD, Blackwell HE (2007) Local and tunable n→π* interactions regulate amide isomerism in the peptoid backbone. J Am Chem Soc 129:8928-8929.
    • (2007) J Am Chem Soc , vol.129 , pp. 8928-8929
    • Gorske, B.C.1    Bastian, B.L.2    Geske, G.D.3    Blackwell, H.E.4
  • 35
    • 33749185744 scopus 로고    scopus 로고
    • Stereoelectronic tuning of the structure and stability of the Trp cage miniprotein
    • Naduthambi D, Zondlo NJ (2006) Stereoelectronic tuning of the structure and stability of the Trp cage miniprotein. J Am Chem Soc 128:12430-12431.
    • (2006) J Am Chem Soc , vol.128 , pp. 12430-12431
    • Naduthambi, D.1    Zondlo, N.J.2
  • 36
    • 41449083869 scopus 로고    scopus 로고
    • Stabilization of the collagen triple helix by O-methylation of hydroxyproline residues
    • Kotch FW, Guzei IA, Raines RT (2008) Stabilization of the collagen triple helix by O-methylation of hydroxyproline residues. J Am Chem Soc 130:2952-2953.
    • (2008) J Am Chem Soc , vol.130 , pp. 2952-2953
    • Kotch, F.W.1    Guzei, I.A.2    Raines, R.T.3
  • 37
    • 32544443339 scopus 로고    scopus 로고
    • Conformational preference and cis-trans isomerization of 4(R)-substituted proline residues
    • Song IK, Kang YK (2006) Conformational preference and cis-trans isomerization of 4(R)-substituted proline residues. J Phys Chem B 110:1915-1927.
    • (2006) J Phys Chem B , vol.110 , pp. 1915-1927
    • Song, I.K.1    Kang, Y.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.