메뉴 건너뛰기




Volumn 26, Issue 2, 1997, Pages 155-162

Crystallization of monoacylated proteins: Influence of acyl chain length

Author keywords

Acylation; Dynamic light scattering; Protein crystallography; Ribonuclease A; Self association

Indexed keywords

RIBONUCLEASE A;

EID: 0030767245     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050067     Document Type: Article
Times cited : (7)

References (33)
  • 2
    • 0028029452 scopus 로고
    • Structure of ribonuclease a derivative II at 2.1 Å resolution
    • Boqué L, Coll MG, Vilanova M, Cuchillo CM, Fita I (1994) Structure of ribonuclease A derivative II at 2.1 Å resolution. J Biol Chem 269:19707-19712
    • (1994) J Biol Chem , vol.269 , pp. 19707-19712
    • Boqué, L.1    Coll, M.G.2    Vilanova, M.3    Cuchillo, C.M.4    Fita, I.5
  • 3
    • 0030565274 scopus 로고    scopus 로고
    • Dynamic light scattering study of precrystallizing ribonuclease solutions
    • Boyer M, Roy M-O, Jullien M (1996) Dynamic light scattering study of precrystallizing ribonuclease solutions. J Crystal Growth 167:212-220
    • (1996) J Crystal Growth , vol.167 , pp. 212-220
    • Boyer, M.1    Roy, M.-O.2    Jullien, M.3
  • 5
    • 84990642430 scopus 로고
    • Applications of electrospray mass spectrometry to studies on the structural properties of Ribonuclease a and Ribonuclease B
    • Camilleri P, Haskins NJ, Rudd PM, Saunders MR (1993) Applications of electrospray mass spectrometry to studies on the structural properties of Ribonuclease A and Ribonuclease B. Rapid Commun. Mass Spec 7:332-335
    • (1993) Rapid Commun. Mass Spec , vol.7 , pp. 332-335
    • Camilleri, P.1    Haskins, N.J.2    Rudd, P.M.3    Saunders, M.R.4
  • 6
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey PJ (1995) Protein lipidation in cell signaling. Science 268:221-225
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 7
    • 0001041039 scopus 로고
    • Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphate
    • Crook EM, Mathias AP, Rabin BR (1960) Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2′:3′-phosphate. Biochem J 74:234-238
    • (1960) Biochem J , vol.74 , pp. 234-238
    • Crook, E.M.1    Mathias, A.P.2    Rabin, B.R.3
  • 8
    • 0026486538 scopus 로고
    • Crystal packing in six crystal forms of pancreatic ribonuclease
    • Crosio M-P, Janin J, Jullien M (1992) Crystal packing in six crystal forms of pancreatic ribonuclease. J Mol Biol 228:243-251
    • (1992) J Mol Biol , vol.228 , pp. 243-251
    • Crosio, M.-P.1    Janin, J.2    Jullien, M.3
  • 9
    • 0026501884 scopus 로고
    • Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs
    • Del Mel VSJ, Martin PD, Doscher MS, Edwards BFP (1992) Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs. J Biol Chem 267: 247-256
    • (1992) J Biol Chem , vol.267 , pp. 247-256
    • Del Mel, V.S.J.1    Martin, P.D.2    Doscher, M.S.3    Edwards, B.F.P.4
  • 10
    • 0002760773 scopus 로고
    • Particle sizing by quasi-elastic light scattering
    • Finsy R (1994) Particle sizing by quasi-elastic light scattering. Adv Colloid Interface Sci 52:79-143
    • (1994) Adv Colloid Interface Sci , vol.52 , pp. 79-143
    • Finsy, R.1
  • 12
    • 0017142274 scopus 로고
    • PK changes of ionizable reporter groups as an index of conformational changes in proteins
    • Garel J-R (1976) PK changes of ionizable reporter groups as an index of conformational changes in proteins. Eur J Biochem 70:179-189
    • (1976) Eur J Biochem , vol.70 , pp. 179-189
    • Garel, J.-R.1
  • 16
    • 0024464493 scopus 로고
    • Lipid modification of proteins and their membrane transport
    • Kabanov AV, Levashov AV, Alakhov VY (1989) Lipid modification of proteins and their membrane transport. Protein Eng 3:39-42
    • (1989) Protein Eng , vol.3 , pp. 39-42
    • Kabanov, A.V.1    Levashov, A.V.2    Alakhov, V.Y.3
  • 17
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W (1988) Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Cryst 21:916-924
    • (1988) J Appl Cryst , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 18
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: The method of cumulants
    • Koppel DE (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. J Chem Phys 57:4814-4820
    • (1972) J Chem Phys , vol.57 , pp. 4814-4820
    • De Koppel1
  • 20
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marschall CJ (1993) Protein prenylation: a mediator of protein-protein interactions. Science 259:1865-1866
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marschall, C.J.1
  • 21
  • 22
    • 0022092648 scopus 로고
    • Improved techniques for particle size determination by quasi-elastic light scattering
    • Morrison ID, Grabowski EF, Herb CA (1985) Improved techniques for particle size determination by quasi-elastic light scattering. Langmuir 1:496-501
    • (1985) Langmuir , vol.1 , pp. 496-501
    • Morrison, I.D.1    Grabowski, E.F.2    Herb, C.A.3
  • 23
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • Peitzsch RM, McLaughlin S (1993) Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins. Biochemistry 32:10436-10443
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 24
    • 0001769895 scopus 로고
    • Particle interactions
    • Pecora R (ed) Plenum, New York
    • Pusey PN, Tough RJA (1985) Particle interactions. In: Pecora R (ed) Dynamic light scattering. Plenum, New York, pp 85-179
    • (1985) Dynamic Light Scattering , pp. 85-179
    • Pusey, P.N.1    Tough, R.J.A.2
  • 25
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh MD (1994) Myristylation and palmitylation of Src family members: the fats of the matter. Cell 76:411-413
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 26
    • 77956909282 scopus 로고
    • Bovine pancreatic ribonuclease
    • Boyer P (ed) Academic Press, New York
    • Richards FM, Wyckoff HW (1971) Bovine pancreatic ribonuclease. In: Boyer P (ed) The enzymes 3rd edn. vol 4. Academic Press, New York, pp 647-806
    • (1971) The Enzymes 3rd Edn. , vol.4 , pp. 647-806
    • Richards, F.M.1    Wyckoff, H.W.2
  • 28
    • 0028276861 scopus 로고
    • Membrane interaction of small N-myristoylated peptides: Implications for membrane anchoring and protein-protein association
    • Sankaram MB (1994) Membrane interaction of small N-myristoylated peptides: implications for membrane anchoring and protein-protein association. Biophys J 67:105-112
    • (1994) Biophys J , vol.67 , pp. 105-112
    • Sankaram, M.B.1
  • 29
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
    • Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M (1995) Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376:444-447
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 30
    • 0023665255 scopus 로고
    • The crystal structure of ribonuclease B at 2.5 Å resolution
    • Williams RL, Greene SM, McPherson A (1987) The crystal structure of ribonuclease B at 2.5 Å resolution. J Biol Chem 262:16020-16031
    • (1987) J Biol Chem , vol.262 , pp. 16020-16031
    • Williams, R.L.1    Greene, S.M.2    McPherson, A.3
  • 32
    • 0028564999 scopus 로고
    • The structure of RNase a complexed with 3̊-CMP and d(CpA): Active site conformation and conserved water molecules
    • Zegers I, Macs D, Dao-Thi M-H, Poortmans F, Palmer R, Wyns L (1994) The structure of RNase A complexed with 3̊-CMP and d(CpA): active site conformation and conserved water molecules. Protein Sci 3:2322-2339
    • (1994) Protein Sci , vol.3 , pp. 2322-2339
    • Zegers, I.1    Macs, D.2    Dao-Thi, M.-H.3    Poortmans, F.4    Palmer, R.5    Wyns, L.6
  • 33
    • 0027429591 scopus 로고
    • Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations
    • Zheng I, Knighton DR, Xuong NH, Taylor SS, Sowadski JM, Ten Eyck LF (1993) Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Sci 2:1559-1573
    • (1993) Protein Sci , vol.2 , pp. 1559-1573
    • Zheng, I.1    Knighton, D.R.2    Xuong, N.H.3    Taylor, S.S.4    Sowadski, J.M.5    Ten Eyck, L.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.